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[ CAS No. 3150-24-1 ] {[proInfo.proName]}

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Chemical Structure| 3150-24-1
Chemical Structure| 3150-24-1
Structure of 3150-24-1 * Storage: {[proInfo.prStorage]}
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Product Details of [ 3150-24-1 ]

CAS No. :3150-24-1 MDL No. :MFCD00063256
Formula : C12H15NO8 Boiling Point : -
Linear Structure Formula :- InChI Key :IFBHRQDFSNCLOZ-YBXAARCKSA-N
M.W : 301.24 Pubchem ID :65115
Synonyms :
p-Nitrophenyl β-D-galactoside;PNPG;NSC 89287;pNPGal;p-Nitrophenyl β-D-Galactopyranoside

Calculated chemistry of [ 3150-24-1 ]

Physicochemical Properties

Num. heavy atoms : 21
Num. arom. heavy atoms : 6
Fraction Csp3 : 0.5
Num. rotatable bonds : 4
Num. H-bond acceptors : 8.0
Num. H-bond donors : 4.0
Molar Refractivity : 69.41
TPSA : 145.2 Ų

Pharmacokinetics

GI absorption : Low
BBB permeant : No
P-gp substrate : No
CYP1A2 inhibitor : No
CYP2C19 inhibitor : No
CYP2C9 inhibitor : No
CYP2D6 inhibitor : No
CYP3A4 inhibitor : No
Log Kp (skin permeation) : -8.45 cm/s

Lipophilicity

Log Po/w (iLOGP) : 0.62
Log Po/w (XLOGP3) : -0.44
Log Po/w (WLOGP) : -1.23
Log Po/w (MLOGP) : -1.86
Log Po/w (SILICOS-IT) : -2.88
Consensus Log Po/w : -1.16

Druglikeness

Lipinski : 0.0
Ghose : None
Veber : 1.0
Egan : 1.0
Muegge : 0.0
Bioavailability Score : 0.55

Water Solubility

Log S (ESOL) : -1.38
Solubility : 12.6 mg/ml ; 0.0419 mol/l
Class : Very soluble
Log S (Ali) : -2.14
Solubility : 2.16 mg/ml ; 0.00718 mol/l
Class : Soluble
Log S (SILICOS-IT) : 0.41
Solubility : 778.0 mg/ml ; 2.58 mol/l
Class : Soluble

Medicinal Chemistry

PAINS : 0.0 alert
Brenk : 2.0 alert
Leadlikeness : 0.0
Synthetic accessibility : 4.12

Safety of [ 3150-24-1 ]

Signal Word:Warning Class:N/A
Precautionary Statements:P261-P305+P351+P338 UN#:N/A
Hazard Statements:H302-H315-H319-H335 Packing Group:N/A
GHS Pictogram:

Application In Synthesis of [ 3150-24-1 ]

* All experimental methods are cited from the reference, please refer to the original source for details. We do not guarantee the accuracy of the content in the reference.

  • Downstream synthetic route of [ 3150-24-1 ]

[ 3150-24-1 ] Synthesis Path-Downstream   1~85

  • 1
  • 4-nitrophenyl 2,3,4,6-tetra-O-acetyl-β-D-galactopyranoside [ No CAS ]
  • [ 3150-24-1 ]
YieldReaction ConditionsOperation in experiment
98% With sodium methylate In methanol for 18h; A 1-(4-nitrophenoxy)-β-D-galactopyranoside (3) 1-(4-nitrophenoxy)-β-D-galactopyranoside (3) 2, 3, 4, 6-tetra-O-acetyl-1-(4-nitrophenoxy)-β-D-galactopyranoside (110 mg, 0.23 mmol) was dissolved in MeOH with a catalytic amount of NaOMe. After 18 h the reaction was quenched with a catalytic amount of DOWEX, filtered and concentrated to give the product as an yellow oily solid in 98% yield (69 mg). 1H-NMR (400 MHz, CDCl3): δ 8.24, 7.35 (2H, m, Ar), 5.71 (1H, d, J1,2=3.3 Hz, H1), 4.03 (1H, dd, J2,1=3.3 Hz, J2,3=9.8 Hz, H2), 4.01 (1H, m, H4), 3.99 (1H, m, H3), 3.85 (1H, app t, J=5.9 Hz, H5), 3.71 (2H, d, J6,5=6.0 Hz, H6). HRMS (EI) calculated for C12H15NO8Na 324.0695. found 324.0709.
With methanol; ammonia
With methanol; sodium methylate at 20℃;
With sodium methylate In methanol at 20℃;

  • 2
  • [ 3150-24-1 ]
  • [ 5094-33-7 ]
YieldReaction ConditionsOperation in experiment
With hydrogen;5% palladium on carbon; In methanol; for 4.0h; p-Nitrophenyl β-D-galactopyranoside (500 mg, 1.659 mmole) was dissolved in dry methanol (30 mL) and a slurry of 5% Palladium on carbon in dry methanol (2 mL, +2×2 mL rinses) added. The reaction flask was evacuated and flushed with hydrogen gas and left to stir under an atmosphere of hydrogen gas for 4 hours. After this time t.l.c. analysis showed the production of a new, ninhydrin positive product (Rf=0.62, SiO2; irrigant=1:2 chloroform:methanol). 1H-n.m.r. (D6-DMSO) was consistent with the p-aminophenyl β-D-galactoside structure expected.
With palladium on activated charcoal; hydrogen; In tetrahydrofuran; methanol; for 48.0h; 1-(4-aminophenoxy)-β-D-galactopyranoside (4) 1-(4-nitrophenoxy)-β-D-galactopyranoside (assumed 70 mg, 0.23 mmol) was dissolved in 1:1 MeOH:THF, a catalytic amount of Pd/C was added and the flask evacuated using a water pump, H2 was introduced and the stirred reaction was allowed to proceed under H2 for 48 h then the H2 was pumped out and air reintroduced. The Pd/C was filtered off and concentrated, NMR analysis revealed that full reduction to the desired amine had not occurred. The product was observed by NMR and mass spec analysis.
  • 3
  • [ 16505-91-2 ]
  • [ 3150-24-1 ]
  • [ 136882-23-0 ]
YieldReaction ConditionsOperation in experiment
29.5% With disodium hydrogenphosphate; 2-amino-2-hydroxymethyl-1,3-propanediol; magnesium chloride at 23℃; for 58h; β-galactosidase;
29% β1,4galactosidase (EC 3.2.1.23, from Escherichia coli);
  • 4
  • N-Acetyl-D-glucosamine [ No CAS ]
  • [ 3150-24-1 ]
  • N-acetyl-D-lactosamine [ No CAS ]
YieldReaction ConditionsOperation in experiment
67% With acetate buffer; β-galactosidase from Bacillus circulans for 1.5h; Ambient temperature;
37% With β-galactosidase from B. circulans In various solvent(s) at 37℃; for 2h; pH=4.5;
20% With crude extract of hepatopancreas of Aplysia fasciata In acetate buffer at 30℃;
11.6% With potassium phosphate buffer In dimethyl sulfoxide at 37℃; for 16h; β-galactosidase from D. pneumoniae;
With Bacillus circulans β-D-galactosidase at 55℃; for 2h;
94 %Chromat. With 1,3-di-n-butoxy-2-methoxypropane; Thermus thermophilus β-galactosidase In aq. phosphate buffer at 60℃; for 3h; Enzymatic reaction; regioselective reaction; Disaccharide synthesis General procedure: Transglycosylation reactions were carried out in 1.0 mL of solution (2 M solvent)-sodium phosphate buffer (50 mM, pH 6.0), with 51.2 mg (0.17 M) pNP-b-Gal (donor) and 188 g (0.85 M) of GlcNAc (acceptor) mixture was preequilibrated to 60 C. Afterwards, 36 mmol min 1 (U) of T. thermophilus b-galactosidase were added to the reaction mixture and reaction was incubated during 3 h, then, was stopped (and homogenized in the case of biphasic systems) by addition of methanol. Reaction yields were determined by HPLC-ELSD. The crude mixture was then directly loaded onto a carboneCelite column eluted with a linear gradient of 0e15% (v/v) of ethanol in water. Solvents were eliminated and disaccharide (LacNAc) was dissolved in D2O to be characterized by 1H and 13C NMR spectroscopy. NMR spectra for LacNAc were consistent to previous reports.

  • 5
  • [ 76-83-5 ]
  • [ 3150-24-1 ]
  • [ 102717-05-5 ]
YieldReaction ConditionsOperation in experiment
84% With pyridine for 48h;
57% With N,N-dimethylamino-pyridine In pyridine; ethyl acetate; triethylamine 1.24.a 1.24.a 1.24.a p-Nitrophenyl 6-O-triphenylmethyl-β-D-galactopyranoside A solution of p-nitrophenyl β-D-galactopyranoside (9.0 g, 30 mmol), chlorotriphenylmethane (16.7 g, 60 mmol) and N,N-dimethylaminopyridine (609 mg, 5 mmol) in absolute pyridine (100 ml) is heated at 60° C. for 4 hours. After concentration in vacuo, the residue is purified by flash chromatography [petroleum ether/ethyl acetate 2:1→3:2, in each case with 0.5% of triethylamine]. Colourless crystals (9.23 g, 57%) are obtained; TLC [methylene chloride/methanol/ammonia (25%) 15:3:0.2]: Rf=0.55; melting point=82° C.
With pyridine for 72h; Ambient temperature;
  • 6
  • [ 58479-61-1 ]
  • [ 3150-24-1 ]
  • [ 110319-37-4 ]
YieldReaction ConditionsOperation in experiment
75% With silver nitrate In N,N-dimethyl-formamide for 48h; Ambient temperature;
  • 7
  • [ 3150-24-1 ]
  • [ 100-02-7 ]
YieldReaction ConditionsOperation in experiment
With β-D-galactosidase; phosphate buffer In water monomer at 37℃; in the presence of 4-amino-4-deoxy-β-D-galactopyranoside or 4-fluoro-4-deoxy-β-D-galactopyranoside;
With β-D-glucosidase of Sclerotium rolfsii In water monomer at 65℃; for 0.5h; enzymic hydrolysis, rate;
With sodium tetraborate; sodium citrate buffer; β-galactosidase at 25℃; for 0.166667h; measuring hydrolytic enzyme activity of β-galactosidase immobilized in a protein film, 1.) pH = 3.5, 2.) pH = 9.8;
With β-glycosidase I (92-95 kDa, from Aspergillus oryzae) In acetate buffer at 40℃; for 0.166667h;
With β-galactosidase I from Japanese persimmon; anhydrous Sodium acetate; bovine serum albumine at 30℃; for 0.166667h;
With β-D-galactosidase (EC 3.2.1.23) from Escherichia coli at 25℃;
With benzenesulfonamide; Averrhoa carambola L. cv. B10 β-galactosidase I; anhydrous trisodium citrate In water monomer at 37℃; for 0.416667h;
With 4-morpholineethanesulfonic acid; lpr mouse monoclonal autoantibody G1-5; MRL-lpr; sodium chloride at 37℃;
With citrate buffer at 37℃;
With Caldicellulosiruptor saccharolyticus β-glucosidase aq. phosphate buffer; Enzymatic reaction;
With Bacillus circulans Biolacta N°5 β-galactosidase at 37℃; for 0.166667h; aq. phosphate buffer; Enzymatic reaction;
With β-glucosidase I from Prunus domestica seeds at 45℃; aq. phosphate buffer; Enzymatic reaction;
With β-galactosidase from Bacillus circulans at 20℃; for 0.0166667h; Microwave irradiation; aq. phosphate buffer; Enzymatic reaction; regioselective reaction;
With dalcochinase F1H96 mutant; anhydrous Sodium acetate at 30℃; Enzymatic reaction; Kinetic measurements General procedure: The catalytic efficiencies (kcat/Km) of the wild-type and mutant forms of dalcochinase for hydrolysis of various pNP-glycoside substrates were determined from progress curves at low substrate concentrations (less than 1/5 Km of wild-type dalcochinase toward the same substrate) in 0.1 M sodium acetate, pH 5.0 at 30 C. The pnitrophenol released was monitored by following the absorbance at 360 nm until substrate depletion was observed. When the substrate concentration is low, the rate of reaction (v) is related to the substrate concentration by the equation:35ν=kcat/Km[E]0[S]. The change in absorbance with respect to time was fitted to first-order rate equation using the program GraFit 5.0 (ErithacusSoftware Limited, Horley, UK) to yield pseudo-first-order rate constant that corresponds to (kcat/Km) [E]0. Since [E]0, which was the concentration of enzyme used in the reaction, was known, the value of kcat/Km could be easily obtained.
With C-terminally His6-tagged Oryza sativa L. β-glucosidase OsTAGG2 In aq. acetate buffer at 37℃; for 0.166667h; Enzymatic reaction;
With Kluyveromyces lactis β-galactosidase; α-cyclodextrine In aq. acetate buffer at 37℃; Enzymatic reaction; 2.6 Determination of molecular mass and KM of β-galactosidase The determination of the β-galactosidase molecular mass was done by gel filtration using Superdex 200 (Amersham Biosciences, UK). The flow rate was 1mlmin-1 and fractions of about 1ml were collected for 152min (buffer: 50mM sodium phosphate pH 6.5+0.15M NaCl). A calibration curve was constructed using bovine serum albumin, ovalbumin, catalase and alcohol dehydrogenase as standards. (0018) The KM value for the substrate pNP-β-d-gal was determined using the Tate and Reynolds method [25]. The solution was buffered at pH 6.5 with 50mM sodium acetate buffer, containing 10mM α-cyclodextrin. The reaction was followed for two min and the increase in absorbance from the complex formation was recorded. From these data, enzyme kinetics were calculated, and Michaelis-Menten and Hanes plots were drawn. Determinations were done in duplicate. The extinction coefficient of pNP in the buffer was determined via Beer-Lambert equation (A= · c · d, where A=absorbance, b=path length (cm) and c=concentration (M)). (0019) The β-galactosidase concentration was determined using a Coomassie stained SDS-PA gel for the calculation of kcat [26].
With C-terminus histidine tagged α-galactosidase from Thermotoga maritima D327G mutant In aq. acetate buffer at 65℃; Green chemistry; Enzymatic reaction;
With β-D-galactosidase immobilized on co-polymer of allyl glycidyl ether and divinyl benzene
With Os4BGlu13 In aq. acetate buffer at 30℃; for 0.25h; Enzymatic reaction; 2.4. Determination of b-glucosidase activity from protein fractions The activities of protein fractions to hydrolyze pNPGlc weretested in a manner similar to previously published methods[27e30]. Aliquots of enzyme solutions were incubated with 4 mMpNPGlc in 50 mM sodium acetate (NaOAc) buffer, pH 5.0, (totalreaction volume 50 ml) at 30 C for 20 min. The reactions werestopped by adding 150 ml of 2 M sodium carbonate (Na2CO3). Thereleased p-nitrophenol (pNP) was quantified by measuring theabsorbance at 405 nm (A405) with a microplate reader (ThermoLabsystems, Helsinki, Finland), and comparing it to that of a pNPstandard curve. The hydrolysis of GA4-GE was determined by asimilar reaction in 50 mM NaOAc, followed with a peroxidase/glucose oxidase-based glucose assay (PGO assay, SigmaeAldrich),as previously described [24]. In all cases, control reactions incubated without b-glucosidase enzyme served as blanks. Proteinconcentrations were determined with a Bio-Rad Bradford assaywith bovine serum albumin (BSA) as a standard.
With Ginkgo biloba seeds β-galactosidase, molecular mass determined by SDS-PAGE under non-reducing condition and under reducing condition: ca. 32 kDa and 16 kDa, resp., containing N-terminal amino acid sequence: H-K-A-N-X-V-T-V-A-F-V-M-T-Q-H- In aq. acetate buffer at 37℃; for 0.5h; Enzymatic reaction;
With Cellulosimicrobium cellulans strain 21 GH1 β-glucosidase CcBgl1B, recombinant, molecular weight: 57 kDa; water monomer In aq. phosphate buffer at 37℃; for 0.166667h; Enzymatic reaction;
With β-galactosidase from Thermotoga maritima; water monomer In aq. phosphate buffer at 75℃; Enzymatic reaction;
With dihydrogen peroxide; C36H38Cl4Cu2N8O2; ascorbic acid In aq. phosphate buffer at 37℃;
With water monomer; β-glucosidase BGL0224 from Oenococcus oeni SD-2a In aq. phosphate buffer at 50℃; for 0.5h; Enzymatic reaction;
With 1-pyrenecarboxylic acid In aq. buffer at 40℃;

Reference: [1]Nam Shin, Jeong E.; Maradufu, Asafu; Marion, Jean; Perlin, Arthur S. [Carbohydrate Research, 1980, vol. 84, p. 328 - 335]
[2]Sadana, Jai C.; Shewale, Jaiprakash G.; Patil, Rajukmar V. [Carbohydrate Research, 1983, vol. 118, p. 205 - 214]
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[6]Tschamber, Theophile; Gessier, Francois; Dubost, Estelle; Newsome, Jeffery; Tarnus, Celine; Kohler, Josiane; Neuburger, Markus; Streith, Jacques [Bioorganic and Medicinal Chemistry, 2003, vol. 11, # 17, p. 3559 - 3568]
[7]Balasubramaniam, Sumathi; Lee, Heng Chin; Lazan, Hamid; Othman, Roohaida; Ali, Zainon Mohd. [Phytochemistry, 2005, vol. 66, # 2, p. 153 - 163]
[8]Lee, Eun-Jung; Jang, Eun-Jung; Lee, Eunhae; Yu, Jaehoon; Chung, Hee Yong; Jang, Young-Ju [Bioorganic and Medicinal Chemistry, 2007, vol. 15, # 5, p. 2016 - 2023]
[9]Ahn, Young Ock; Zheng, Meiying; Bevan, David R.; Esen, Asim; Shiu, Shin-Han; Benson, Jonas; Peng, Hsiao-Ping; Miller, Joseph T.; Cheng, Chi-Lien; Poulton, Jonathan E.; Shih, Ming-Che [Phytochemistry, 2007, vol. 68, # 11, p. 1510 - 1520]
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[11]Location in patent: experimental part Perez-Sanchez, Maria; Sandoval, Manuel; Cortes-Cabrera, Alvaro; Garcia-Marin, Hector; Sinisterra, Jose V.; Garcia, Jose I.; Hernaiz, Maria J. [Green Chemistry, 2011, vol. 13, # 10, p. 2810 - 2817]
[12]Location in patent: experimental part Chen, Lei; Li, Ning; Zong, Min-Hua [Process Biochemistry, 2012, vol. 47, # 1, p. 127 - 132]
[13]Location in patent: experimental part Kamerke, Claudia; Pattky, Martin; Huhn, Carolin; Elling, Lothar [Journal of Molecular Catalysis B: Enzymatic, 2012, vol. 79, p. 27 - 34]
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  • 8
  • [ 3150-24-1 ]
  • [ 100-02-7 ]
  • [ 7296-64-2 ]
YieldReaction ConditionsOperation in experiment
With galactanase from Penicillium citrinum In water at 40℃; acetate buffer, pH 4.5; activity of galactanase, also in the presence of HgCl2, KCl, and various metal ions;
With recombinant β-D-galactosidase from Paenibacillus thiaminolyticus, histidine-tagged protein at 37℃; for 0.166667h; aq. phosphate buffer; Enzymatic reaction;
With β-D-galactosidase from Penicillium sp.; water In aq. acetate buffer at 37℃; Enzymatic reaction; One unit of the β-D-galactosidase activity towards p-nitrophenyl β-D-galactopyranoside (pNPbGal) was defined as the amount of the enzyme required to hydrolyze 1 mM of the substrate per 1 min at 37 °C in 50 mM sodium acetate buffer, pH 5.0.
  • 9
  • [ 3150-24-1 ]
  • [ 59-23-4 ]
YieldReaction ConditionsOperation in experiment
37% With Escherichia coli β-galactosidase; N-acetyl-D-glucosamine In glycerol at 30℃; aq. buffer; regioselective reaction; 4.4. General procedure for transglycosylation reactions using β-galactosidase from E. coli General procedure: A solution of 100 mg (0.17 M) p-NP-β-d-Gal (donor) and 550 mg (1.25 M) of N-acetylglucosamine (acceptor) in 1 mL of glycerol-based solvent (2 M)-buffer mixture was pre-equilibrated to 30 °C. Afterwards, 155 μmol/min (U) of β-galactosidase from E. coli were added to the reaction mixture. Reaction was monitored by HPLC UV-vis and final products obtained by HPLC with a light scattering detector (ELSD) were analysed. The reaction was stopped by heating to 100 °C for 5 min. Final reaction mixture obtained was loaded on activated carbon (50% m/m) and Celite (50% m/m) column (50 cm×2 cm, 25 cm column height) eluted with 3 volumes of milliQ water, 3 volumes of 5% ethanol (in water) and 3 volumes of 15% ethanol (in water). Disaccharide enriched fractions were determined by TLC on silica gel 60 (Merck, Darmstadt, Germany), with isopropanol/nitromethane/water (10:9:2) as eluent with detection by spraying the plates with 10% aq H2SO4 in methanol and heating. Ten, these fractions were collected in 15% ethanol; they were pooled and analysed by HPLC-ELSD as described above. 1H NMR spectrum (D2O) was recorded to purified disaccharide on a Bruker 500 MHz spectrometer.
With acetate buffer; Aspergillus niger β-D-galactosidase at 37℃; for 0.333333h; substrate specifity studies with various D-galactose containing saccharides;
With acetate buffer at 37℃; for 0.5h;
  • 10
  • [ 10521-91-2 ]
  • [ 3150-24-1 ]
  • 5-Phenylpentyl β-D-galactopyranoside [ No CAS ]
YieldReaction ConditionsOperation in experiment
72% With lipid-coated β-D-galactosidase In carbon dioxide at 40℃; for 3h;
71% With β-D-glycosidase I from Pyrococcus furiosus; lipid coated In di-isopropyl ether at 30℃;
In di-isopropyl ether at 30℃; for 48h; Yield given;
With β-D-galactosidase In trifluoromethan at 37℃;

  • 11
  • [ 3150-24-1 ]
  • [ 220934-98-5 ]
YieldReaction ConditionsOperation in experiment
77% With galactose-oxidase; catalase In various solvent(s) at 4℃; for 24h;
  • 12
  • [ 122331-70-8 ]
  • [ 3150-24-1 ]
  • [ 167554-00-9 ]
YieldReaction ConditionsOperation in experiment
50% With acetate buffer (pH: 5.0) at 22℃; for 7h;
  • 13
  • [ 6734-33-4 ]
  • [ 3150-24-1 ]
  • [ 133972-95-9 ]
  • 4-methyl-2-oxo-2H-chromen-7-yl O-β-D-galactopyranosyl-(1->3)-β-D-xylopyranoside [ No CAS ]
YieldReaction ConditionsOperation in experiment
1: 16.7% 2: 4.6% In phosphate buffer at 37℃; for 4h;
With β-D-galactosidase (EC 3.2.1.23; E. coli); Triton X-100 at 32℃; for 4h; phosphate buffer pH 7.3; Yield given. Yields of byproduct given;
  • 15
  • [ 64650-83-5 ]
  • [ 3150-24-1 ]
  • [ 110879-61-3 ]
YieldReaction ConditionsOperation in experiment
67% With bovine testes β-galactosidase; McIlvain buffer In water at 37℃; for 50h;
67% With β-galactosidase from bovine testis In aq. phosphate buffer at 37 - 90℃; for 50h; Enzymatic reaction; regioselective reaction; Transgalactosylation with β-galactosidase (bovine testis)(General procedure 1, GP 1) General procedure: Both donor (1 equiv) and acceptor substrates (10 equiv) were dissolved in McIlvaine buffer (50 mM, pH 4.3) and warmed to 37°C. β-Galactosidase (bovine testis, 4.7 U/mmol acceptor; assay Ref. 9) was added and incubated for 50 h at 37°C. For termination the enzyme was denatured by heating to 90°C for 10 min. In case of p-nitrophenyl hexopyranoside donors the resulting p-nitro phenol was extracted with ethyl acetate. Separation and purification of the products were done by gel chromatography on Biogel P2 eluting first with ammonium hydrogen carbonate buffer and then with deionized water. Remaining buffer salts were removed using a short mixed bed ion exchange column.
22% With β-galactosidase from bovine testes; sodium phosphate-citrate buffer at 37℃; for 48h; pH 4.3;
67 % Chromat. With McIlvain buffer at 37℃; for 50h; Enzymatic reaction;

  • 16
  • [ 188641-24-9 ]
  • [ 3150-24-1 ]
  • [ 188641-26-1 ]
YieldReaction ConditionsOperation in experiment
68% With KPB buffer In N,N-dimethyl-formamide at 37℃; for 4.5h; in the presence of β1-3 galactosidase from Bacillus circulans;
  • 17
  • N-Acetyl-D-glucosamine [ No CAS ]
  • [ 3150-24-1 ]
  • lacto-N-biose [ No CAS ]
YieldReaction ConditionsOperation in experiment
97% With β-GaL-3-NTag from B. circulans ATCC 31382; 3-butyl-1-methyl-1H-imidazol-3-ium hexafluorophosphate In aq. phosphate buffer at 37℃; for 3h; Enzymatic reaction; 4.4. Transgalactosylation reactions General procedure: pNP-β-Gal (85 mM) and GlcNAc or GalNAc (425 mM) were dissolved in 1.00 ml of buffer sodium phosphate 50 mM pH 6 and different percentages of ILs, and pre-warmed at reaction temperature (37 °C). Reaction started by addition of biocatalyst to the mixture: 5 U of recombinant enzyme. Aliquots (50 μl) were withdrawn from reaction media at different times. The reaction was stopped after 3 h by heating to 100 °C for 5 min and conserved immediately at -20 °C. Analytical determination of products were performed by HPLC using an NH2P50-4E amino column (Asahipak, Japan) using three detectors: ELSD (Evaporative Light Scattering), UV-vis at 317 nm and CD (Circular Dichroism). Each experimental assay was determined at least three times with standard deviation under 5% of the average of samples.
95% With 2-hydroxy-N,N-dimethyl-propanamide; β-galactosidase-3-N-terminal 6-histidine tag from Bacillus circulans ATCC 31382 In aq. phosphate buffer at 37 - 100℃; Green chemistry; Enzymatic reaction; regioselective reaction;
75% With β-Gal-3 ATCC 31382 immoblized on monofunctional glyoxyl agarose In aq. phosphate buffer at 37℃; for 3h; Ionic liquid; Enzymatic reaction; regioselective reaction;
22.4% With sodium acetate; β-galactosidase In acetonitrile at 37℃; for 5h;

  • 18
  • [ 6082-22-0 ]
  • [ 3150-24-1 ]
  • [ 75669-79-3 ]
YieldReaction ConditionsOperation in experiment
66% With bovine testes β-galactosidase; McIlvain buffer In water at 37℃; for 50h;
53% With sodium phosphate; β-galactosidase In water; N,N-dimethyl-formamide at 37℃; for 3h;
  • 19
  • [ 108-24-7 ]
  • [ 3150-24-1 ]
  • 4-nitrophenyl 2,3,4,6-tetra-O-acetyl-β-D-galactopyranoside [ No CAS ]
YieldReaction ConditionsOperation in experiment
99% With pyridine for 5h; cooling;
98% With iodine at 20℃; for 15h;
91% With pyridine; dmap In pyridine at 20℃; for 16h; Inert atmosphere;
91% With pyridine; dmap at 20℃; for 16h; Inert atmosphere; I.j j) 4-(Azidoacetamido)phenyl 2,3,4,6-tetra-O-acetyl-β-D-galactopyranoside (“12”) [0159] In a 250 mL round-bottom flask containing 11 (4.07 g, 13.51 mmol) and DMAP (20 mg) was added 50 mL of pyridine under argon. Then, 35 mL of Ac2O was added dropwise. The mixture was stirred at r.t. for 16 hrs. The crude mixture was diluted in EtOAc (800 mL) and washed with HCl 1N (2×300 mL), saturated NaHCO3 (2×300 mL), water (2×300 mL) and brine (300 mL). After drying (Na2SO4) and concentration, the residue crystallized from PE and was filtered and dried to afford 5.75 g of the pure acetylated intermediate (91%). Then, in a 1 L round-bottom flask containing the acetylated p-nitrophenyl-galactopyranoside, freshly distilled CH2Cl2 was added under argon atmosphere. The mixture was degassed with 3 vacuum/argon cycles. Then, 0.634 mg (0.60 mmol, 0.05 eq.) of Pd/C (10 wt %) was added and the mixture was submitted to 3 others vacuum/argon cycles. The solution was subjected to hydrogen atmosphere by 3 vacuum/hydrogen cycles and stirred at r.t. for 16 hrs. The reduction of the nitro group can be monitored by TLC (PE/EtOAc, 1:1). After total disappearance of starting material, the mixture was flushed with argon, cooled to 0° C., and Et3N (2.0 mL, 14.32 mmol, 1.2 eq.) was added. Bromoacetylbromide (1.24 mL, 14.32 mmol, 1.2 eq.) was added dropwise and the mixture was stirred for 1 hr at 0° C. The mixture was allowed to warm up at r.t. for 1 h and was filtered through a plug of celite (CH2Cl2) to remove Pd/C. The crude mixture in CH2Cl2 (600 mL) was washed with HCl 1N (2×250 mL), water (2×250 mL) and brine (250 mL). After drying (Na2SO4), concentration and total removal of CH2Cl2 with high vacuum, the crude bromide derivative (pale yellow solid) was dissolved in anhydrous DMF (80 mL). Sodium azide (4.1 g, 62.6 mmol, 5 eq.) and tetra-n-butyl ammonium iodide (0.46 g, 1.25 mmol, 0.1 eq.) was added, and the mixture was stirred at 50° C. under argon for 16 hrs. The mixture was cooled to r.t., filtered and the solid was washed with EtOAc. The filtrate was diluted with EtOAc to reach a total volume of 600 mL. The organic layer was washed with aq. NaHCO3 (2×200 mL), water (2×200 mL), brine (200 mL) and dried. After concentration, the residue (pale yellow solid) was purified by silica gel column chromatography (PE/EtOAc, 1:1) followed by crystallization (CH2Cl2/PE) to afford the azido-functionalized glycoside 12 as a white solid (5.229 g, 74% over 4 steps). [0160] Rf=0.29 (PE/EtOAc, 1:1). [α]D=+6.6° (c=1.3, CH2Cl2). [0161] ESI-MS (positive mode) m/z: 545.0 [M+Na]+, 1066.4 [2M+Na]+ HR-ESI-MS (positive mode) m/z: calcd for C22H26N4NaO11 [M+Na]+ 545.1496, found 545.1496
In pyridine
With pyridine at 20℃; for 16h; Inert atmosphere; I.j j) 4-(Azidoacetamido)phenyl 2,3,4,6-tetra-0-acetyl-[3-D-galactopyranoside ("12")In a 250 mL round-bottom flask containing 11 (4.07 g, 13.51 mmol) and DMAP (20 mg) was added 50 mL of pyridine under argon. Then, 35 mL of Ac20 was added dropwise. The mixture was stirred at r.t. for 16 hrs. The crude mixture was diluted in EtOAc (800 mL) and washed with HCI 1 N (2x300 mL), saturated NaHC03 (2x300 mL), water (2x300 mL) and brine (300 mL). After drying (Na2S04) and concentration, the residue crystallized from PE and was filtered and dried to afford 5.75 g of the pure acetylated intermediate (91 %). Then, in a 1 L round-bottom flask containing the acetylated p-nitrophenyl-galactopyranoside, freshly distilled CH2CI2 was added under argon atmosphere. The mixture was degassed with 3 vacuum/argon cycles. Then, 0.634 mg (0.60 mmol, 0.05 eq.) of Pd/C (10 wt%) was added and the mixture was submitted to 3 others vacuum/argon cycles. The solution was subjected to hydrogen atmosphere by 3 vacuum/hydrogen cycles and stirred at r.t. for 16 hrs. The reduction of the nitro group can be monitored by TLC (PE/EtOAc, 1 :1 ). After total disappearance of starting material, the mixture was flushed with argon, cooled to 0°C, and Et3N (2.0 mL, 14.32 mmol, 1.2 eq.) was added. Bromoacetylbromide (1.24 mL, 14. 32 mmol, 1 .2 eq.) was added dropwise and the mixture was stirred for 1 hr at 0°C. The mixture was allowed to warm up at r.t. for 1 h and was filtered through a plug of celite (CH2CI2) to remove Pd/C. The crude mixture in CH2CI2 (600 mL) was washed with HCI 1 N (2x250 mL), water (2x250 mL) and brine (250 mL). After drying (Na2S04), concentration and total removal of CH2CI2 with high vacuum, the crude bromide derivative (pale yellow solid) was dissolved in anhydrous DMF (80 mL). Sodium azide (4.1 g, 62.6 mmol, 5 eq.) and tetra-n-butyl ammonium iodide (0.46 g, 1.25 mmol, 0.1 eq.) was added, and the mixture was stirred at 50°C under argon for 16 hrs. The mixture was cooled to r.t., filtered and the solid was washed with EtOAc. The filtrate was diluted with EtOAc to reach a total volume of 600 mL. The organic layer was washed with aq. NaHC03 (2x200 mL), water (2x200 mL), brine (200 mL) and dried. After concentration, the residue (pale yellow solid) was purified by silica gel column chromatography (PE/EtOAc, 1 :1 ) followed by crystallization (CH2CI2/PE) to afford the azido-functionalized glycoside 12 as a white solid (5.229 g, 74% over 4 steps).Rf = 0.29 (PE/EtOAc, 1 :1 ). [a]D = + 6.6 ° (c = 1.3, CH2CI2).ESI-MS (positive mode) m/z: 545.0 [M + Na]+, 1066.4 [2M + Na]+ HR-ESI-MS (positive mode) m/z: calcd for C22H26N4NaOn [M + Na]+ 545.1496, found 545.1496

  • 20
  • [ 195531-55-6 ]
  • [ 3150-24-1 ]
  • [ 81573-30-0 ]
  • [ 195531-59-0 ]
YieldReaction ConditionsOperation in experiment
1: 61% 2: 6% With bovine β-galactosidase In phosphate buffer at 37℃; for 60h; Enzymatic reaction;
  • 21
  • [ 3150-24-1 ]
  • [ 3459-18-5 ]
  • N-{(2S,3R,4R,5S,6R)-2-[(2R,3R,4R,5R,6S)-4,5-Dihydroxy-2-hydroxymethyl-6-(4-nitro-phenoxy)-tetrahydro-pyran-3-yloxy]-4,5-dihydroxy-6-hydroxymethyl-tetrahydro-pyran-3-yl}-acetamide [ No CAS ]
YieldReaction ConditionsOperation in experiment
1.9% With N-acetyl-β-hexosaminidase (Aspergillus oryzae) at 25℃;
  • 22
  • [ 48149-72-0 ]
  • [ 3150-24-1 ]
  • allyl β-D-galactopyranosyl-(1->4)-α-D-galactopyranoside [ No CAS ]
  • 23
  • [ 16758-34-2 ]
  • [ 3150-24-1 ]
  • phenyl β-D-galactopyranosyl-(1->4)-1-thio-β-D-galactopyranoside [ No CAS ]
YieldReaction ConditionsOperation in experiment
63% With sodium phosphate In acetonitrile at 30℃; for 72h;
  • 24
  • allyl 2-acetamido-2-deoxy-β-D-glucopyranoside [ No CAS ]
  • [ 3150-24-1 ]
  • allyl β-D-galactopyranosyl-(1->4)-2-acetamido-2-deoxy-β-D-glucopyranoside [ No CAS ]
YieldReaction ConditionsOperation in experiment
30% With sodium phosphate In acetonitrile at 30℃; for 72h;
  • 25
  • [ 54400-75-8 ]
  • [ 3150-24-1 ]
  • allyl β-D-galactopyranosyl-(1->4)-2-acetamido-2-deoxy-α-D-glucopyranoside [ No CAS ]
YieldReaction ConditionsOperation in experiment
66% With sodium phosphide In water; acetonitrile at 30℃; for 72h;
  • 26
  • [ 2595-07-5 ]
  • [ 3150-24-1 ]
  • allyl β-D-galactopyranosyl-(1->4)-β-D-galactopyranoside [ No CAS ]
YieldReaction ConditionsOperation in experiment
49% With sodium phosphate In acetonitrile at 30℃; for 72h;
  • 27
  • [ 14131-68-1 ]
  • [ 3150-24-1 ]
  • [ 183811-88-3 ]
YieldReaction ConditionsOperation in experiment
93% With Escherichia coli β-galactosidase In (1,3-bis(2,2,2-trifluoroethoxy)propan-2-ol) at 30℃; aq. buffer; regioselective reaction; 4.4. General procedure for transglycosylation reactions using β-galactosidase from E. coli General procedure: A solution of 100 mg (0.17 M) p-NP-β-d-Gal (donor) and 550 mg (1.25 M) of N-acetylglucosamine (acceptor) in 1 mL of glycerol-based solvent (2 M)-buffer mixture was pre-equilibrated to 30 °C. Afterwards, 155 μmol/min (U) of β-galactosidase from E. coli were added to the reaction mixture. Reaction was monitored by HPLC UV-vis and final products obtained by HPLC with a light scattering detector (ELSD) were analysed. The reaction was stopped by heating to 100 °C for 5 min. Final reaction mixture obtained was loaded on activated carbon (50% m/m) and Celite (50% m/m) column (50 cm×2 cm, 25 cm column height) eluted with 3 volumes of milliQ water, 3 volumes of 5% ethanol (in water) and 3 volumes of 15% ethanol (in water). Disaccharide enriched fractions were determined by TLC on silica gel 60 (Merck, Darmstadt, Germany), with isopropanol/nitromethane/water (10:9:2) as eluent with detection by spraying the plates with 10% aq H2SO4 in methanol and heating. Ten, these fractions were collected in 15% ethanol; they were pooled and analysed by HPLC-ELSD as described above. 1H NMR spectrum (D2O) was recorded to purified disaccharide on a Bruker 500 MHz spectrometer.
With β-galactosidase In phosphate buffer at 37℃; for 10h;
With Bacillus circulans Biolacta N°5 β-galactosidase In (1,3-bis(2,2,2-trifluoroethoxy)propan-2-ol) at 30℃; aq. buffer; Enzymatic reaction; regioselective reaction;
  • 28
  • [ 3971-45-7 ]
  • [ 3150-24-1 ]
  • [ 317321-20-3 ]
YieldReaction ConditionsOperation in experiment
36% With B. circulans β-galactosidase In acetate buffer at 25℃; for 28h; Enzymatic reaction;
  • 29
  • [ 7512-17-6 ]
  • [ 3150-24-1 ]
  • [ 13071-21-1 ]
YieldReaction ConditionsOperation in experiment
86% With Biolacta N5; In N,N-dimethylhexanamide; at 30℃;pH 5;aq. buffer; Enzymatic reaction; General procedure: A solution of 51.2 mg (0.17 M) p-nitrophenyl-beta-d-galactopyranoside (donor) and 188 mg (0.85 M) of N-acetylglucosamine (acceptor) in 1 mL of green solvent (2 M)-buffer mixture was pre-equilibrated to 30 C. Afterwards, 155 mumol/min (U) of beta-galactosidase were added to the reaction mixture. Reaction was monitored by HPLC UV-vis and final products analysed by HPLC with an evaporative light scattering detector (ELSD). The reaction was stopped by heating the sample at 100 C for 5 min.Isolation of disaccharides was done by carbon/Celite (50% m/m), chromatography, the column was eluted with milliQ water and ethanol gradient (from 5% to 15% v/v). [21] and [26] The structures of the disaccharides (Gal-beta(1?4)GlcNAc and Gal-beta(1?6)GlcNAc) were assigned by 1H and 13C NMR (D2O, 700 MHz), spectra were identical to previous references. [21], [26] and [27]In order to determine the effect of non-proteic substances present in Biolacta preparation in the reaction yield, transglycosylation reactions were carried out using semipurified (lyophilized) enzyme. The best performing solvents were chosen in view of the previous results, using crude extracts and setting the reactions with semipurified enzymes. The transglycosylation conditions were the same mentioned above and the reaction was monitored using HPLC-ELSD.For functionalized disaccharides the same protocol previously described was used, and different glycoconjugates as acceptors were added. A solution of 51.2 mg (0.17 M) pNP-beta-Gal (donor) and the different monosaccharides functionalized 1 and 2 (0.51 M).
  • 30
  • [ 3615-17-6 ]
  • [ 3150-24-1 ]
  • N-[(1S,2R,3S,4R)-1-Formyl-2,3,4-trihydroxy-5-((2R,3R,4S,5R,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-pentyl]-acetamide [ No CAS ]
YieldReaction ConditionsOperation in experiment
With triethyl phosphate; sodium acetate In water at 30℃; Enzymatic reaction;
  • 31
  • [ 3615-17-6 ]
  • [ 3150-24-1 ]
  • N-[(1S,2R,3S,4R)-1-Formyl-2,3,4-trihydroxy-5-((2R,3R,4S,5R,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-pentyl]-acetamide [ No CAS ]
  • N-[(1S,2R,3S,4R)-1-Formyl-2,4,5-trihydroxy-3-((2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-pentyl]-acetamide [ No CAS ]
YieldReaction ConditionsOperation in experiment
With triethyl phosphate; sodium acetate In water at 30℃;
  • 32
  • [ 134-61-2 ]
  • [ 3150-24-1 ]
  • [ 72142-81-5 ]
  • [ 82535-18-0 ]
  • 33
  • [ 10284-63-6 ]
  • [ 3150-24-1 ]
  • 1D-1-O-(β-D-Galactopyranosyl)-4-O-methyl-chiro-inositol [ No CAS ]
  • 1D-1-O-(β-D-Galactopyranosyl-(1->4)-O-β-D-galactopyranosyl)-4-O-methyl-chiro-inositol [ No CAS ]
  • 34
  • [ 220069-61-4 ]
  • [ 3150-24-1 ]
  • p-nitrophenyl (β-D-glucopyranosyl)-(1->3)-(β-D-glucopyranosyl)-(1->3)-β-D-galactopyranoside [ No CAS ]
YieldReaction ConditionsOperation in experiment
89% With mutated (1,3)-β-D-glucan endohydrolase Glu231Gly In phosphate buffer at 37℃;
  • 35
  • [ 3150-24-1 ]
  • [ 184908-98-3 ]
YieldReaction ConditionsOperation in experiment
98% With copper(I) sulfate; oxygen; copper(II) sulfate; catalase In phosphate buffer at 20℃; for 24h;
With Dactylius dendroides galactose oxidase (E.C. 1.1.3.9); oxygen; catalase In phosphate buffer for 72h;
  • 36
  • [ 98-59-9 ]
  • [ 3150-24-1 ]
  • [ 704892-96-6 ]
YieldReaction ConditionsOperation in experiment
59% With pyridine at 0 - 20℃; for 4.5h;
59% With pyridine at -10 - 20℃; for 3h; p-Nitrophenyl β-D-galactopyranoside (1, 1.0 g, 3.32 mmol) dissolved in anhydrous pyridine (20 mL) was treated at -10°C with p-toluene sulfonic acid chloride (633 mg, 3.32 mmol) dissolved in anhydrous pyridine (2 mL) and then stirred for 3 h at room temperature. The mixture was quenched with water (60 mL) and extracted with ethyl acetate. The combined organic phases were washed with diluted HCl and water, and then dried over Mg2SO4. After evaporation the raw material was purified on silica (dichloromethane/methanol 17:1) to give 896 mg (59%) of 18 as a colorless solid. Mp 81°C; [α]D20 126 (c 0.6, MeOH). 1H NMR (400 MHz, MeOD): d 8.16 (m, 2H, Ar-3/5), 7.72 (m, 2H,Ar0-2/6), 7.29 (m, 2H, Ar0-3/5), 7.15 (m, 2H, Ar-2/6), 4.98 (d, 1H,J1,2 = 7.6 Hz, H-1), 4.30 (dd, 1H, J5,6a = 4.3, J6a,6b = 10.7 Hz, H-6a),4.26 (dd, 1H, J5,6b = 7.6, J6a,6b = 10.7 Hz, H-6b), 4.04 (dd, 1H,J5,6a = 4.3, J5,6b = 7.6 Hz, H-5), 3.87 (bd, 1H, J3,4 = 3.3 Hz, H-4), 3.74(dd, 1H, J1,2 = 7.6, J2,3 = 9.7 Hz, H-2), 3.60 (dd, 1H, J2,3 = 9.7,J3,4 = 3.3 Hz, H-3), 2.37 (s, 3H, CH3). 13C NMR (100.6 MHz, MeOD):d 164.10 (Ar-1), 146.96 (Ar0-1), 144.28 (Ar0-4), 134.69 (Ar-4),131.37 (2C, Ar0-3/5), 129.40 (2C, Ar0-2/6), 126.97 (2C, Ar-3/5),118.11 (2C, Ar-2/6), 102.14 (C-1), 74.76 (C-5), 74.72 (C-3), 72.08(C-2), 71.17 (C-6), 70.35 (C-4), 21.94 (CH3).Calcd for C19H21NO10S (455.44): C, 50.11; H, 4.65; N, 3.08; S,7.04. Found: C, 49.95; H, 4.89; N, 2.91; S, 7.09.
52% With pyridine
51% With pyridine at 20℃; for 2h;

  • 37
  • [ 10284-63-6 ]
  • [ 3150-24-1 ]
  • 1D-1-O-(β-D-Galactopyranosyl)-4-O-methyl-chiro-inositol [ No CAS ]
  • 1D-1-O-(β-D-galactopyranosyl)-3-O-methyl-chiro-inisitol [ No CAS ]
  • 38
  • [ 40617-59-2 ]
  • [ 3150-24-1 ]
  • 1D-1-O-(β-D-galactopyranosyl)-3,4-di-O-methyl-chiro-inisitol [ No CAS ]
YieldReaction ConditionsOperation in experiment
52% With β-galactosidase from Thermoanaerobacter sp In phosphate buffer at 37℃; for 72h;
  • 39
  • [ 3971-47-9 ]
  • [ 3150-24-1 ]
  • (2R,3R,4S,5R,6R)-2-((2R,3R,4R)-3-Hydroxy-2-hydroxymethyl-tetrahydro-pyran-4-yloxy)-6-hydroxymethyl-tetrahydro-pyran-3,4,5-triol [ No CAS ]
YieldReaction ConditionsOperation in experiment
81% With bovine testea β-galactosidase; McIlvain buffer In water at 37℃; for 50h;
  • 40
  • [ 869496-43-5 ]
  • [ 3150-24-1 ]
  • [ 124501-67-3 ]
YieldReaction ConditionsOperation in experiment
70% With bovine testes β-galactosidase; McIlvain buffer In water at 37℃; for 50h;
  • 41
  • [ 869361-50-2 ]
  • [ 3150-24-1 ]
  • [ 869361-55-7 ]
YieldReaction ConditionsOperation in experiment
81% With bovine testes β-galactosidase; McIlvain buffer In water at 37℃; for 50h;
  • 42
  • [ 2106-10-7 ]
  • [ 3150-24-1 ]
  • 4-nitrophenyl β-D-glucopyranosyl-(1->3)-β-D-galactopyranoside [ No CAS ]
  • 43
  • [ 530-26-7 ]
  • [ 113-24-6 ]
  • [ 3150-24-1 ]
  • 4-nitrophenyl O-(3-deoxy-D-glycero-α-D-galacto-2-nonulopyranosylonic acid)-(2->3)-O-β-D-galactopyranose [ No CAS ]
YieldReaction ConditionsOperation in experiment
75% With tPm0188Ph; cytidine triphosphate; magnesium chloride In various solvents at 37℃; for 2h;
  • 44
  • [ 6082-04-8 ]
  • [ 3150-24-1 ]
  • [ 85193-95-9 ]
YieldReaction ConditionsOperation in experiment
61% With potassium phosphate buffer; β-galactosidase (B. circulans) In acetonitrile at 20℃; for 36h;
  • 45
  • [ 98-88-4 ]
  • [ 3150-24-1 ]
  • [ 643758-55-8 ]
YieldReaction ConditionsOperation in experiment
58% With pyridine at -20℃;
With pyridine In dichloromethane; water; N,N-dimethyl-formamide 1 p-Nitrophenyl 2,3,6-tri-O-benzoyl-β-D-galactopyranoside (1) p-Nitrophenyl 2,3,6-tri-O-benzoyl-β-D-galactopyranoside (1) Benzoyl chloride (1.50 ml, 1.82 g, 12.9 mmol) was added dropwise to a solution of p-nitrophenyl β-D-galactopyranoside (1.00 g, 3.32 mmol) in DMF (15 ml) and pyridine (15 ml) at -20° C. After stirring for 5 h at -5° C. another 0.30 ml of benzoyl chloride (0.36 g, 2.59 mmol) was added dropwise, and the solution was stirred for 2 h at -5° C. Water (10 ml) was added and the mixture was concentrated by evaporation in vacuo. The residue was dissolved in CH2Cl2, and the organic phase was washed sequentially with saturated aqueous NaHCO3, 1 M HCl and brine, dried over MgSO4, filtered and concentrated in vacuo. Column chromatography (toluene→4:1 toluene/EtOAc) followed by crystallization from hot toluene yielded 1 (850 mg, 1.39 mmol, 42%); mp 180-181° C.; 1H-NMR (400 MHz): δH (CDCl3): 8.05 (m, 2 H, Ar), 8.0-7.3 (m, 15 H, 3xBz), 7.06 (m, 2 H, Ar), 6.10 (dd, 1 H, J2,3 10.3 Hz, J2,1 7.9 Hz, H-2), 5.48 (dd, 1 H, J3,2 10.3 Hz, J3,4 3.2 Hz, H-3), 5.40 (d, 1 H, J1,2 7.9 Hz, H-1), 4.76 (dd, 1 H, J6,6 11.7 Hz, J6,5 5.1 Hz, H-6), 4.68 (dd, 1 H, J6,6 11.7 Hz, J6,5 7.7 Hz, H-6), 4.47 (m, 1 H, H-4), 4.31 (m, 1 H, H-5), 2.66 (d, 1 H, JOH,4 4.5 Hz, OH); 13C-NMR (75 MHz): δC (CDCl3): 166.4, 165.8, 165.3, 161.3, 143.0, 133.7, 133.5, 129.9, 129.7, 129.7, 129.3, 129.0, 128.6, 128.6, 128.5, 128.5, 125.6, 116.8, 98.8, 73.9, 73.2, 69.0, 67.1, 63.0; ESI-MS: m/z=636.5 [M+Na]+ (expected for C33H27NO11Na+: m/z=636.2).
  • 46
  • [ 3150-24-1 ]
  • [ 75-50-3 ]
  • p-nitrophenyl 6-O-sulfo-β-D-galactopyranoside trimethylamine salt [ No CAS ]
YieldReaction ConditionsOperation in experiment
68% With sulfur trioxide In N,N-dimethyl-formamide at 40℃; for 1.5h;
  • 47
  • [ 3150-24-1 ]
  • [ 704892-97-7 ]
YieldReaction ConditionsOperation in experiment
Multi-step reaction with 2 steps 1: 63 percent / pyridine / 5.5 h / 0 °C 2: 39 percent / sodium azide / dimethylformamide / 5 h / 80 °C
Multi-step reaction with 2 steps 1: 51 percent / pyridine / 2 h / 20 °C 2: 60 percent / sodium azide / dimethylformamide / 14 h / 80 °C
Multi-step reaction with 2 steps 1: 59 percent / pyridine / 4.5 h / 0 - 20 °C 2: 87 percent / sodium azide / dimethylformamide / 70 °C
Multi-step reaction with 2 steps 1: 63 percent / pyridine 2: 39 percent / NaN3 / dimethylformamide
Multi-step reaction with 2 steps 1: 52 percent / pyridine 2: 60 percent / NaN3 / dimethylformamide

  • 48
  • [ 3150-24-1 ]
  • (2R,3S,4S,5R,6S)-2-(acetoxymethyl)-6-(4-aminophenoxy)tetrahydro-2H-pyran-3,4,5-triyl triacetate [ No CAS ]
YieldReaction ConditionsOperation in experiment
Multi-step reaction with 2 steps 1: 99 percent / pyridine / 5 h / cooling 2: 74 percent / H2 / Pd/C / ethyl acetate / 4 h / 20 °C
Multi-step reaction with 2 steps 1: pyridine 2: 85 percent / H2 / Pd/C / methanol / 3 h / 20 °C
Multi-step reaction with 2 steps 1: pyridine / dmap / 16 h / 20 °C / Inert atmosphere 2: hydrogen / palladium 10% on activated carbon / dichloromethane / 16 h / 20 °C
Multi-step reaction with 2 steps 1: pyridine; dmap / pyridine / 16 h / 20 °C / Inert atmosphere 2: palladium 10% on activated carbon; hydrogen / dichloromethane / 16 h / 20 °C / Inert atmosphere
Multi-step reaction with 2 steps 1: dmap; pyridine / 16 h / 20 °C / Inert atmosphere 2: palladium 10% on activated carbon; hydrogen / dichloromethane / 16 h / 20 °C / Inert atmosphere

  • 49
  • [ 3150-24-1 ]
  • [ 133972-94-8 ]
YieldReaction ConditionsOperation in experiment
Multi-step reaction with 4 steps 1: 16.7 percent / β-D-galactosidase (EC 3.2.1.23; Escherichia coli) / aq. phosphate buffer / 4 h / 37 °C / pH 7.3 2: 89.8 percent / celite-immobilized lipase (EC 3.1.1.3; Amano PS) / tetrahydrofuran / 12 h / 20 °C 3: 15.8 percent / β-D-galactosidase (EC 3.2.1.23; Escherichia coli) / aq. phosphate buffer / 5 h / 37 °C / pH 7.3 4: 85 percent / K2CO3 / methanol / 2 h / 20 °C
Multi-step reaction with 2 steps 1: 15.8 percent / β-D-galactosidase (EC 3.2.1.23; Escherichia coli) / aq. phosphate buffer / 5 h / 37 °C / pH 7.3 2: 85 percent / K2CO3 / methanol / 2 h / 20 °C
Multi-step reaction with 4 steps 1: β-D-galactosidase (EC 3.2.1.23; E. coli), Triton X-100 / 4 h / 32 °C / phosphate buffer pH 7.3 2: 10 percent / DIEA / dimethylformamide 3: 11 percent / β-D-galactosidase (EC 3.2.1.23; E. coli) / 4 h / 32 °C / phosphate buffer pH 7.3 4: 86 percent / aq. c.c. HCl / methanol
Multi-step reaction with 2 steps 1: 11 percent / β-D-galactosidase (EC 3.2.1.23; E. coli) / 4 h / 32 °C / phosphate buffer pH 7.3 2: 86 percent / aq. c.c. HCl / methanol

  • 50
  • [ 1069-87-0 ]
  • [ 3150-24-1 ]
  • 1,2-O-dioctanoyl-3-O-(β-D-galactopyranosyl)glycerol [ No CAS ]
YieldReaction ConditionsOperation in experiment
83% With Aspergillus oryzae, β-galactosidase In water; dimethyl sulfoxide at 25℃; for 24h; 22 Preparation of a Dioctanoyl Glycerol Galactoside Conjugate Enzymatic synthesis of the 3-O-β-D-galactoside was performed using a modification of the procedure of Kren, et al. (Kren, et al., 1992) that employs the β-galactosidase enzyme from Aspergillus oryzae reported to provide higher yields of galactosides from lipophilic aglycones. [00170] 1,2-di-octyl-rac-glycerol (DOG) (65 mg, 0.19 mmole) was dissolved in dimethylsulfoxide (100 mL). p-Nitrophenyl β-D-galactopyranoside (ONPG) (150 mg, 0.50 mmole) was dissolved in 0.1 M Na2HPO4/0.01M MgCl2 buffer, pH 7.0 (4.0 mL) and Tris buffer (pH 7.3, 1.0 mL) was added. The ONPG solution was added slowly to the DOG solution, with vortex mixing, and the solution warmed to 45° C. to dissolve. After cooling, β-galactosidase from Aspergillus oryzae (172 U) was added and the reaction mixture slowly rotated at 25° C. for 24 hours. The reaction mixture was applied directly to a column of Silicagel G (70-230 mesh, 20 g) and eluted by gradient elution using 0-20% methanol in hexanes as eluent. Fractions containing the second major product to elute from the column were combined and evaporated to give a white solid (80 mg, 83% theoretical yield).
  • 51
  • [ 70476-82-3 ]
  • [ 3150-24-1 ]
  • mitoxantrone di-galactoside conjugate [ No CAS ]
YieldReaction ConditionsOperation in experiment
at 25℃; for 24h; 24 B Preparation of a Mitoxantrone Di-Galactoside Conjugate Method B: p-Nitrophenyl β-D-galactopyranoside (150 mg, 0.50 mmole) was dissolved in 0.1 M Na2HPO4/0.01 M MgCl2 buffer, pH 7.0 (4.0 mL) and Tris buffer (pH 7.3, 1.0 mL) was added. Mitoxantrone, dihydrochloride salt (50 mg, 0.11 mmole) was added, and the mixture vortex mixed for 3 min. E. coli β-Galactosidase (172 μL of a 500 U/mL solution in water, 86 U total) was added and the solution rotated slowly at 25° C. for 24 hours. T.l.c. analysis (SiO2 plate, irrigant=8:2:1:0.1 isopropanol:water:triethylamine:acetic acid) indicated product formation. Purification is carried out by preparative t.l.c using the similar systems to those employed in Method A above, to give the title compound
  • 52
  • [ 100-39-0 ]
  • [ 3150-24-1 ]
  • [ 183879-18-7 ]
YieldReaction ConditionsOperation in experiment
81% With di(n-butyl)tin oxide In 1,4-dioxane 1.26.a 1.26.a 1.26.a p-Nitrophenyl 3-O-benzyl-β-D-galactopyranoside Dibutyltin oxide (1.87 g, 7.5 mmol) is added to a solution of p-nitrophenyl β-D-galactopyranoside (1.5 g, 5.0 mmol) in absolute dioxane (40 ml) and the mixture is heated under reflux. After 3 hours, benzyl bromide (3.6 ml, 30 mmol) are added to the solution obtained and the batch is stirred under reflux for a further 48 hours. The solvent is then distilled off in vacuo and the residue is purified by flash chromatography (ethyl acetate/petroleum ether 2:1→1:1]. Colourless crystals (1.58 g 81%) are obtained; TLC [methylene chloride/methanol/ammonia (25%) 15:3:0.2]: Rf=0.69; melting point=127° C.
With tetrabutylammomium bromide; di(n-butyl)tin oxide; N-ethyl-N,N-diisopropylamine In neat (no solvent) at 70℃; for 2.5h; regioselective reaction;
  • 53
  • [ 75-36-5 ]
  • [ 3150-24-1 ]
  • [ 183880-65-1 ]
YieldReaction ConditionsOperation in experiment
47% With pyridine In acetonitrile 1.53.a 1.53.a 1.53.a p-Nitrophenyl 6-O-acetyl-β-D-galactopyranoside A freshly prepared solution of pyridine (2 ml, 25 mmol) and acetyl chloride (1.85 ml, 26 mmol) in acetonitrile (20 ml) is added dropwise to a solution of p-nitrophenyl β-D-galactopyranoside (7.53 g, 25 mmol) in absolute acetonitrile (80 ml) at 0° C. The mixture is stirred at 0° C. for 30 minutes and then concentrated in vacuo. After flash chromatography [methylene chloride/methanol 50:1→20:1], colourless crystals (4.02 g, 47%) are obtained; TLC [methylene chloride/methanol/ammonia (25%) 15:3:0.2]: Rf=0.50.
  • 54
  • [ 96-32-2 ]
  • [ 3150-24-1 ]
  • p-Nitrophenyl 3-O-methoxycarbonylmethyl-α-D-galactopyranoside [ No CAS ]
YieldReaction ConditionsOperation in experiment
43% With tetra-(n-butyl)ammonium iodide; di(n-butyl)tin oxide In 1,4-dioxane 1.42.a 1.42.a 1.42.a p-Nitrophenyl 3-O-methoxycarbonylmethyl-α-D-galactopyranoside Dibutyltin oxide (9.3 g, 37.5 mmol) is added to a solution of p-nitrophenyl β-D-galactopyranoside (7.53 g, 25 mmol) in absolute dioxane (180 ml) and the mixture is heated under reflux. After 4 hours, methyl bromoacetate (8.3 ml, 90 mmol) and tetrabutylammonium iodide (9.25 g, 25 mmol) are added to the solution obtained and the batch is stirred under reflux for a further 3 hours. The solvent is then distilled off in vacuo and the residue is purified by flash chromatography [methylene chloride/methanol 50:1→20:1]. In addition to some by-products, the compound 1.42.a is obtained as colourless crystals (4.05 g, 43%); TLC [methylene chloride/methanol/ammonia (25%) 15:3:0.2]: Rf=0.54; [α]20=-62.0° (c=1.0/CH3OH); melting point 176° C.
  • 55
  • [ 3150-24-1 ]
  • [ 183879-14-3 ]
YieldReaction ConditionsOperation in experiment
84% With di(n-butyl)tin oxide In methanol 1.25.a 1.25.a 1.25.a p-Nitrophenyl 3-O-methyl-β-D-galactopyranoside Dibutyltin oxide (1.87 g, 7.5 mmol) is added to a solution of p-nitrophenyl β-D-galactopyranoside (1.5 g, 5.0 mmol) in absolute methanol (40 ml) and the mixture is heated under reflux. After 3 hours, it is concentrated in vacuo and the residue is dried under an oil pump vacuum for 1 hour. It is taken up in absolute dioxane (40 ml), methyl iodide (1.9 ml, 30 mmol) is added to the resulting solution and the batch is stirred at a bath temperature of 100° C. for 16 hours. The solvent is then distilled off in vacuo and the residue is purified by flash chromatography [ethyl acetate/petroleum ether 2:1→ethyl acetate]. Colourless crystals (1.32 g, 84%) are obtained; TLC [methylene chloride/methanol/ammonia (25%) 15:3:0.2]: Rf=0.34; melting point=196° C.; [α]20=-53.3° (c=1.0/CH3OH).
  • 56
  • [ 3150-24-1 ]
  • [ 145204-48-4 ]
YieldReaction ConditionsOperation in experiment
59% 1.38.a 1.38.a 1.38.a p-Nitrophenyl 2,3,4,6-tetra-O-methyl-β-D-galactopyranoside p-Nitrophenyl β-D-galactopyranoside (904 mg, 3 mmol) is methylated as described in Example 1.24.c. After flash chromatography [petroleum ether/ethyl acetate 8:1→6:1→4:1→2:1], a colourless, waxy solid (633 mg, 59%) is obtained; TLC [ethyl acetate]: Rf=0.67; [α]20=-55.7° (c=0.9/CH2Cl2).
  • 57
  • palladium-on-active charcoal [ No CAS ]
  • [ 3150-24-1 ]
  • [ 5094-33-7 ]
YieldReaction ConditionsOperation in experiment
78% In methanol; water; EXAMPLE 1.23 p-Aminophenyl β-D-galactopyranoside p-Nitrophenyl β-D-galactopyranoside (3.0 g, 10 mmol) is dissolved in methanol/water 1:1 (50 ml) and, after addition of palladium-on-active charcoal (10% of Pd, 200 mg), hydrogenation is carried out in a hydrogen atmosphere under a slightly increased pressure for 3 hours. The suspension is filtered over Celite and the material on the filter is washed with hot methanol/water 1:1 (100 ml). Concentration of the filtrate in vacuo and recrystallization from methanol gives colourless crystals (2.11 g, 78%); TLC [methanol]: Rf=0.62; [α]20=-39.5 (c=1.0/H2O); melting point=166 C.
  • 58
  • N-methoxyacetate-D-mannosamine [ No CAS ]
  • [ 113-24-6 ]
  • [ 3150-24-1 ]
  • 4-nitrophenyl O-[5-(2-methoxyacetamido)-3,5-dideoxy-D-glycero-α-D-galacto-2-nonulopyranosylonic acid]-(2->3)-O-β-D-galactopyranoside [ No CAS ]
YieldReaction ConditionsOperation in experiment
93% With Neisseria meningitidis CMP-sialic acid synthetase; Pasteurella multocida sialyltransferase 1; Pasturella multocida sialic acid aldolase; magnesium chloride; cytidine 5'-triphosphate disodium salt In water at 37℃; aq. Tris-HCl buffer; Enzymatic reaction;
  • 59
  • N-methoxyacetate-D-mannosamine [ No CAS ]
  • [ 113-24-6 ]
  • [ 3150-24-1 ]
  • 4-nitrophenyl O-[5-(2-methoxyacetamido)-3,5-dideoxy-D-glycero-α-D-galacto-2-nonulopyranosylonic acid]-(2->6)-O-β-D-galactopyranoside [ No CAS ]
YieldReaction ConditionsOperation in experiment
97% With Neisseria meningitidis CMP-sialic acid synthetase; Pasturella multocida sialic acid aldolase; Photobacterium damsela α2-6-sialyltransferase; magnesium chloride; cytidine 5'-triphosphate disodium salt In water at 37℃; aq. Tris-HCl buffer; Enzymatic reaction;
  • 60
  • [ 27552-09-6 ]
  • [ 113-24-6 ]
  • [ 3150-24-1 ]
  • 4-nitrophenyl O-[3-deoxy-5-O-methyl-D-glycero-α-D-galacto-2-nonulopyranosylonic acid]-(2->3)-O-β-D-galactopyranoside [ No CAS ]
YieldReaction ConditionsOperation in experiment
81% With Neisseria meningitidis CMP-sialic acid synthetase; Pasteurella multocida sialyltransferase 1; Pasturella multocida sialic acid aldolase; magnesium chloride; cytidine 5'-triphosphate disodium salt In water at 37℃; aq. Tris-HCl buffer; Enzymatic reaction;
  • 61
  • [ 27552-09-6 ]
  • [ 113-24-6 ]
  • [ 3150-24-1 ]
  • 4-nitrophenyl O-[3-deoxy-5-O-methyl-D-glycero-α-D-galacto-2-nonulopyranosylonic acid]-(2->6)-O-β-D-galactopyranoside [ No CAS ]
YieldReaction ConditionsOperation in experiment
84% With Neisseria meningitidis CMP-sialic acid synthetase; Pasturella multocida sialic acid aldolase; Photobacterium damsela α2-6-sialyltransferase; magnesium chloride; cytidine 5'-triphosphate disodium salt In water at 37℃; aq. Tris-HCl buffer; Enzymatic reaction;
  • 62
  • [ 113-24-6 ]
  • [ 97604-58-5 ]
  • [ 3150-24-1 ]
  • 4-nitrophenyl O-[5-azido-3,5-dideoxy-D-glycero-α-D-galacto-2-nonulopyranosylonic acid]-(2->3)-O-β-D-galactopyranoside [ No CAS ]
YieldReaction ConditionsOperation in experiment
87% With Neisseria meningitidis CMP-sialic acid synthetase; Pasteurella multocida sialyltransferase 1; Pasturella multocida sialic acid aldolase; magnesium chloride; cytidine 5'-triphosphate disodium salt In water at 37℃; aq. Tris-HCl buffer; Enzymatic reaction;
  • 63
  • [ 113-24-6 ]
  • [ 97604-58-5 ]
  • [ 3150-24-1 ]
  • 4-nitrophenyl O-[5-azido-3,5-dideoxy-D-glycero-α-D-galacto-2-nonulopyranosylonic acid]-(2->6)-O-β-D-galactopyranoside [ No CAS ]
YieldReaction ConditionsOperation in experiment
87% With Neisseria meningitidis CMP-sialic acid synthetase; Pasturella multocida sialic acid aldolase; Photobacterium damsela α2-6-sialyltransferase; magnesium chloride; cytidine 5'-triphosphate disodium salt In water at 37℃; aq. Tris-HCl buffer; Enzymatic reaction;
  • 64
  • [ 113-24-6 ]
  • 2-deoxy-2-fluoro-D-mannopyranoside [ No CAS ]
  • [ 3150-24-1 ]
  • 4-nitrophenyl O-[3,5-dideoxy-5-fluoro-D-glycero-α-D-galacto-2-nonulopyranosylonic acid]-(2->3)-O-β-D-galactopyranoside [ No CAS ]
YieldReaction ConditionsOperation in experiment
74% With Neisseria meningitidis CMP-sialic acid synthetase; Pasteurella multocida sialyltransferase 1; Pasturella multocida sialic acid aldolase; magnesium chloride; cytidine 5'-triphosphate disodium salt In water at 37℃; aq. Tris-HCl buffer; Enzymatic reaction;
  • 65
  • [ 113-24-6 ]
  • 2-deoxy-2-fluoro-D-mannopyranoside [ No CAS ]
  • [ 3150-24-1 ]
  • 4-nitrophenyl O-[3,5-dideoxy-5-fluoro-D-glycero-α-D-galacto-2-nonulopyranosylonic acid]-(2->6)-O-β-D-galactopyranoside [ No CAS ]
YieldReaction ConditionsOperation in experiment
79% With Neisseria meningitidis CMP-sialic acid synthetase; Pasturella multocida sialic acid aldolase; Photobacterium damsela α2-6-sialyltransferase; magnesium chloride; cytidine 5'-triphosphate disodium salt In water at 37℃; aq. Tris-HCl buffer; Enzymatic reaction;
  • 66
  • [ 113-24-6 ]
  • 2-deoxy-2-(fluoroacetamido)-D-mannose [ No CAS ]
  • [ 3150-24-1 ]
  • 4-nitrophenyl O-[5-(2-fluoroacetamido)-3,5-dideoxy-D-glycero-α-D-galacto-2-nonulopyranosylonic acid]-(2->3)-O-β-D-galactopyranoside [ No CAS ]
YieldReaction ConditionsOperation in experiment
91% With Neisseria meningitidis CMP-sialic acid synthetase; Pasteurella multocida sialyltransferase 1; Pasturella multocida sialic acid aldolase; magnesium chloride; cytidine 5'-triphosphate disodium salt In water at 37℃; aq. Tris-HCl buffer; Enzymatic reaction;
  • 67
  • [ 113-24-6 ]
  • 2-deoxy-2-(fluoroacetamido)-D-mannose [ No CAS ]
  • [ 3150-24-1 ]
  • 4-nitrophenyl O-[5-(2-fluoroacetamido)-3,5-dideoxy-D-glycero-α-D-galacto-2-nonulopyranosylonic acid]-(2->6)-O-β-D-galactopyranoside [ No CAS ]
YieldReaction ConditionsOperation in experiment
96% With Neisseria meningitidis CMP-sialic acid synthetase; Pasturella multocida sialic acid aldolase; Photobacterium damsela α2-6-sialyltransferase; magnesium chloride; cytidine 5'-triphosphate disodium salt In water at 37℃; aq. Tris-HCl buffer; Enzymatic reaction;
  • 68
  • [ 113-24-6 ]
  • [ 3150-24-1 ]
  • 2-(azidoacetamido)-2-deoxy-D-mannopyranose [ No CAS ]
  • 4-nitrophenyl O-[5-(2-azidoacetamido)-3,5-dideoxy-D-glycero-α-D-galacto-2-nonulopyranosylonic acid]-(2->3)-O-β-D-galactopyranoside [ No CAS ]
YieldReaction ConditionsOperation in experiment
92% With Neisseria meningitidis CMP-sialic acid synthetase; Pasteurella multocida sialyltransferase 1; Pasturella multocida sialic acid aldolase; magnesium chloride; cytidine 5'-triphosphate disodium salt In water at 37℃; aq. Tris-HCl buffer; Enzymatic reaction;
  • 69
  • [ 113-24-6 ]
  • [ 3150-24-1 ]
  • 2-(azidoacetamido)-2-deoxy-D-mannopyranose [ No CAS ]
  • 4-nitrophenyl O-[5-(2-azidoacetamido)-3,5-dideoxy-D-glycero-α-D-galacto-2-nonulopyranosylonic acid]-(2->6)-O-β-D-galactopyranoside [ No CAS ]
YieldReaction ConditionsOperation in experiment
95% With Neisseria meningitidis CMP-sialic acid synthetase; Pasturella multocida sialic acid aldolase; Photobacterium damsela α2-6-sialyltransferase; magnesium chloride; cytidine 5'-triphosphate disodium salt In water at 37℃; aq. Tris-HCl buffer; Enzymatic reaction;
  • 70
  • [ 98-88-4 ]
  • [ 3150-24-1 ]
  • [ 1262015-29-1 ]
YieldReaction ConditionsOperation in experiment
61% Stage #1: 4-nitrophenyl-β-D-galactopyranoside With di(n-butyl)tin oxide In methanol for 2h; Reflux; Stage #2: benzoyl chloride In toluene at 0 - 20℃; Under N2 atmosphere;
  • 71
  • [ 14131-68-1 ]
  • [ 3150-24-1 ]
  • [ 183811-88-3 ]
  • [ 59-23-4 ]
YieldReaction ConditionsOperation in experiment
1: 68% 2: 24% With Escherichia coli β-galactosidase at 30℃; aq. buffer; regioselective reaction; 4.4. General procedure for transglycosylation reactions using β-galactosidase from E. coli General procedure: A solution of 100 mg (0.17 M) p-NP-β-d-Gal (donor) and 550 mg (1.25 M) of N-acetylglucosamine (acceptor) in 1 mL of glycerol-based solvent (2 M)-buffer mixture was pre-equilibrated to 30 °C. Afterwards, 155 μmol/min (U) of β-galactosidase from E. coli were added to the reaction mixture. Reaction was monitored by HPLC UV-vis and final products obtained by HPLC with a light scattering detector (ELSD) were analysed. The reaction was stopped by heating to 100 °C for 5 min. Final reaction mixture obtained was loaded on activated carbon (50% m/m) and Celite (50% m/m) column (50 cm×2 cm, 25 cm column height) eluted with 3 volumes of milliQ water, 3 volumes of 5% ethanol (in water) and 3 volumes of 15% ethanol (in water). Disaccharide enriched fractions were determined by TLC on silica gel 60 (Merck, Darmstadt, Germany), with isopropanol/nitromethane/water (10:9:2) as eluent with detection by spraying the plates with 10% aq H2SO4 in methanol and heating. Ten, these fractions were collected in 15% ethanol; they were pooled and analysed by HPLC-ELSD as described above. 1H NMR spectrum (D2O) was recorded to purified disaccharide on a Bruker 500 MHz spectrometer.
1: 15% 2: 58% With Escherichia coli β-galactosidase In 1,3-bis(2,2,3,3,4,4,4-heptafluorobutoxy)-2-propanol at 30℃; aq. buffer; regioselective reaction; 4.4. General procedure for transglycosylation reactions using β-galactosidase from E. coli General procedure: A solution of 100 mg (0.17 M) p-NP-β-d-Gal (donor) and 550 mg (1.25 M) of N-acetylglucosamine (acceptor) in 1 mL of glycerol-based solvent (2 M)-buffer mixture was pre-equilibrated to 30 °C. Afterwards, 155 μmol/min (U) of β-galactosidase from E. coli were added to the reaction mixture. Reaction was monitored by HPLC UV-vis and final products obtained by HPLC with a light scattering detector (ELSD) were analysed. The reaction was stopped by heating to 100 °C for 5 min. Final reaction mixture obtained was loaded on activated carbon (50% m/m) and Celite (50% m/m) column (50 cm×2 cm, 25 cm column height) eluted with 3 volumes of milliQ water, 3 volumes of 5% ethanol (in water) and 3 volumes of 15% ethanol (in water). Disaccharide enriched fractions were determined by TLC on silica gel 60 (Merck, Darmstadt, Germany), with isopropanol/nitromethane/water (10:9:2) as eluent with detection by spraying the plates with 10% aq H2SO4 in methanol and heating. Ten, these fractions were collected in 15% ethanol; they were pooled and analysed by HPLC-ELSD as described above. 1H NMR spectrum (D2O) was recorded to purified disaccharide on a Bruker 500 MHz spectrometer.
  • 72
  • [ 1363273-29-3 ]
  • [ 3150-24-1 ]
  • C21H39NO16 [ No CAS ]
  • C21H39NO16 [ No CAS ]
YieldReaction ConditionsOperation in experiment
1: 27% 2: 50% With Biolacta N5 at 30℃; aq. buffer; Enzymatic reaction; regioselective reaction; 4.5. General procedure for transglycosylation reactions using glycoconjugates General procedure: A solution of 51.2 mg (0.17 M) p-nitrophenyl-β-d-galactopyranoside (donor) and 188 mg (0.85 M) of N-acetylglucosamine (acceptor) in 1 mL of green solvent (2 M)-buffer mixture was pre-equilibrated to 30 °C. Afterwards, 155 μmol/min (U) of β-galactosidase were added to the reaction mixture. Reaction was monitored by HPLC UV-vis and final products analysed by HPLC with an evaporative light scattering detector (ELSD). The reaction was stopped by heating the sample at 100 °C for 5 min.Isolation of disaccharides was done by carbon/Celite (50% m/m), chromatography, the column was eluted with milliQ water and ethanol gradient (from 5% to 15% v/v). [21] and [26] The structures of the disaccharides (Gal-β(1→4)GlcNAc and Gal-β(1→6)GlcNAc) were assigned by 1H and 13C NMR (D2O, 700 MHz), spectra were identical to previous references. [21], [26] and [27]In order to determine the effect of non-proteic substances present in Biolacta preparation in the reaction yield, transglycosylation reactions were carried out using semipurified (lyophilized) enzyme. The best performing solvents were chosen in view of the previous results, using crude extracts and setting the reactions with semipurified enzymes. The transglycosylation conditions were the same mentioned above and the reaction was monitored using HPLC-ELSD.For functionalized disaccharides the same protocol previously described was used, and different glycoconjugates as acceptors were added. A solution of 51.2 mg (0.17 M) pNP-β-Gal (donor) and the different monosaccharides functionalized 1 and 2 (0.51 M).
1: 34% 2: 19% With Biolacta N5 In 2-hydroxy-N,N-dimethyl-propanamide at 30℃; aq. buffer; Enzymatic reaction; regioselective reaction; 4.5. General procedure for transglycosylation reactions using glycoconjugates General procedure: A solution of 51.2 mg (0.17 M) p-nitrophenyl-β-d-galactopyranoside (donor) and 188 mg (0.85 M) of N-acetylglucosamine (acceptor) in 1 mL of green solvent (2 M)-buffer mixture was pre-equilibrated to 30 °C. Afterwards, 155 μmol/min (U) of β-galactosidase were added to the reaction mixture. Reaction was monitored by HPLC UV-vis and final products analysed by HPLC with an evaporative light scattering detector (ELSD). The reaction was stopped by heating the sample at 100 °C for 5 min.Isolation of disaccharides was done by carbon/Celite (50% m/m), chromatography, the column was eluted with milliQ water and ethanol gradient (from 5% to 15% v/v). [21] and [26] The structures of the disaccharides (Gal-β(1→4)GlcNAc and Gal-β(1→6)GlcNAc) were assigned by 1H and 13C NMR (D2O, 700 MHz), spectra were identical to previous references. [21], [26] and [27]In order to determine the effect of non-proteic substances present in Biolacta preparation in the reaction yield, transglycosylation reactions were carried out using semipurified (lyophilized) enzyme. The best performing solvents were chosen in view of the previous results, using crude extracts and setting the reactions with semipurified enzymes. The transglycosylation conditions were the same mentioned above and the reaction was monitored using HPLC-ELSD.For functionalized disaccharides the same protocol previously described was used, and different glycoconjugates as acceptors were added. A solution of 51.2 mg (0.17 M) pNP-β-Gal (donor) and the different monosaccharides functionalized 1 and 2 (0.51 M).
  • 73
  • [ 7512-17-6 ]
  • [ 3150-24-1 ]
  • [ 13071-21-1 ]
  • [ 32181-59-2 ]
YieldReaction ConditionsOperation in experiment
91%; 9% With Biolacta N5; In 2-hydroxy-1,3-dioxane; at 30℃;pH 5;aq. buffer; Enzymatic reaction; General procedure: A solution of 51.2 mg (0.17 M) p-nitrophenyl-beta-d-galactopyranoside (donor) and 188 mg (0.85 M) of N-acetylglucosamine (acceptor) in 1 mL of green solvent (2 M)-buffer mixture was pre-equilibrated to 30 C. Afterwards, 155 mumol/min (U) of beta-galactosidase were added to the reaction mixture. Reaction was monitored by HPLC UV-vis and final products analysed by HPLC with an evaporative light scattering detector (ELSD). The reaction was stopped by heating the sample at 100 C for 5 min.Isolation of disaccharides was done by carbon/Celite (50% m/m), chromatography, the column was eluted with milliQ water and ethanol gradient (from 5% to 15% v/v). [21] and [26] The structures of the disaccharides (Gal-beta(1?4)GlcNAc and Gal-beta(1?6)GlcNAc) were assigned by 1H and 13C NMR (D2O, 700 MHz), spectra were identical to previous references. [21], [26] and [27]In order to determine the effect of non-proteic substances present in Biolacta preparation in the reaction yield, transglycosylation reactions were carried out using semipurified (lyophilized) enzyme. The best performing solvents were chosen in view of the previous results, using crude extracts and setting the reactions with semipurified enzymes. The transglycosylation conditions were the same mentioned above and the reaction was monitored using HPLC-ELSD.For functionalized disaccharides the same protocol previously described was used, and different glycoconjugates as acceptors were added. A solution of 51.2 mg (0.17 M) pNP-beta-Gal (donor) and the different monosaccharides functionalized 1 and 2 (0.51 M).
17%; 83% With Biolacta N5; at 30℃;pH 5;aq. buffer; Enzymatic reaction; General procedure: A solution of 51.2 mg (0.17 M) p-nitrophenyl-beta-d-galactopyranoside (donor) and 188 mg (0.85 M) of N-acetylglucosamine (acceptor) in 1 mL of green solvent (2 M)-buffer mixture was pre-equilibrated to 30 C. Afterwards, 155 mumol/min (U) of beta-galactosidase were added to the reaction mixture. Reaction was monitored by HPLC UV-vis and final products analysed by HPLC with an evaporative light scattering detector (ELSD). The reaction was stopped by heating the sample at 100 C for 5 min.Isolation of disaccharides was done by carbon/Celite (50% m/m), chromatography, the column was eluted with milliQ water and ethanol gradient (from 5% to 15% v/v). [21] and [26] The structures of the disaccharides (Gal-beta(1?4)GlcNAc and Gal-beta(1?6)GlcNAc) were assigned by 1H and 13C NMR (D2O, 700 MHz), spectra were identical to previous references. [21], [26] and [27]In order to determine the effect of non-proteic substances present in Biolacta preparation in the reaction yield, transglycosylation reactions were carried out using semipurified (lyophilized) enzyme. The best performing solvents were chosen in view of the previous results, using crude extracts and setting the reactions with semipurified enzymes. The transglycosylation conditions were the same mentioned above and the reaction was monitored using HPLC-ELSD.For functionalized disaccharides the same protocol previously described was used, and different glycoconjugates as acceptors were added. A solution of 51.2 mg (0.17 M) pNP-beta-Gal (donor) and the different monosaccharides functionalized 1 and 2 (0.51 M).
  • 74
  • N-Acetyl-D-glucosamine [ No CAS ]
  • [ 3150-24-1 ]
  • N-acetyl-D-lactosamine [ No CAS ]
  • [ 81573-30-0 ]
YieldReaction ConditionsOperation in experiment
1: 22 %Chromat. 2: 78 %Chromat. With 1-n-butoxy-3-methoxy-2-propanol; Thermus thermophilus β-galactosidase In aq. phosphate buffer at 60℃; for 3h; Enzymatic reaction; regioselective reaction; Disaccharide synthesis General procedure: Transglycosylation reactions were carried out in 1.0 mL of solution (2 M solvent)-sodium phosphate buffer (50 mM, pH 6.0), with 51.2 mg (0.17 M) pNP-b-Gal (donor) and 188 g (0.85 M) of GlcNAc (acceptor) mixture was preequilibrated to 60 C. Afterwards, 36 mmol min 1 (U) of T. thermophilus b-galactosidase were added to the reaction mixture and reaction was incubated during 3 h, then, was stopped (and homogenized in the case of biphasic systems) by addition of methanol. Reaction yields were determined by HPLC-ELSD. The crude mixture was then directly loaded onto a carboneCelite column eluted with a linear gradient of 0e15% (v/v) of ethanol in water. Solvents were eliminated and disaccharide (LacNAc) was dissolved in D2O to be characterized by 1H and 13C NMR spectroscopy. NMR spectra for LacNAc were consistent to previous reports.
  • 75
  • N-Acetyl-D-glucosamine [ No CAS ]
  • [ 3150-24-1 ]
  • N-acetyl-D-lactosamine [ No CAS ]
  • [ 81573-30-0 ]
  • [ 80321-98-8 ]
YieldReaction ConditionsOperation in experiment
1: 73 %Chromat. 2: 10 %Chromat. 3: 17 %Chromat. With Thermus thermophilus β-galactosidase In aq. phosphate buffer at 60℃; for 3h; Enzymatic reaction; Disaccharide synthesis General procedure: Transglycosylation reactions were carried out in 1.0 mL of solution (2 M solvent)-sodium phosphate buffer (50 mM, pH 6.0), with 51.2 mg (0.17 M) pNP-b-Gal (donor) and 188 g (0.85 M) of GlcNAc (acceptor) mixture was preequilibrated to 60 C. Afterwards, 36 mmol min 1 (U) of T. thermophilus b-galactosidase were added to the reaction mixture and reaction was incubated during 3 h, then, was stopped (and homogenized in the case of biphasic systems) by addition of methanol. Reaction yields were determined by HPLC-ELSD. The crude mixture was then directly loaded onto a carboneCelite column eluted with a linear gradient of 0e15% (v/v) of ethanol in water. Solvents were eliminated and disaccharide (LacNAc) was dissolved in D2O to be characterized by 1H and 13C NMR spectroscopy. NMR spectra for LacNAc were consistent to previous reports.
  • 76
  • N-Acetyl-D-glucosamine [ No CAS ]
  • [ 3150-24-1 ]
  • [ 10257-28-0 ]
  • N-acetyl-D-lactosamine [ No CAS ]
  • [ 81573-30-0 ]
YieldReaction ConditionsOperation in experiment
1: 33 %Chromat. 2: 7 %Chromat. 3: 55 %Chromat. With glycerol formal; Thermus thermophilus β-galactosidase In aq. phosphate buffer at 60℃; for 3h; Enzymatic reaction; regioselective reaction; Disaccharide synthesis General procedure: Transglycosylation reactions were carried out in 1.0 mL of solution (2 M solvent)-sodium phosphate buffer (50 mM, pH 6.0), with 51.2 mg (0.17 M) pNP-b-Gal (donor) and 188 g (0.85 M) of GlcNAc (acceptor) mixture was preequilibrated to 60 C. Afterwards, 36 mmol min 1 (U) of T. thermophilus b-galactosidase were added to the reaction mixture and reaction was incubated during 3 h, then, was stopped (and homogenized in the case of biphasic systems) by addition of methanol. Reaction yields were determined by HPLC-ELSD. The crude mixture was then directly loaded onto a carboneCelite column eluted with a linear gradient of 0e15% (v/v) of ethanol in water. Solvents were eliminated and disaccharide (LacNAc) was dissolved in D2O to be characterized by 1H and 13C NMR spectroscopy. NMR spectra for LacNAc were consistent to previous reports.
  • 77
  • N-Acetyl-D-glucosamine [ No CAS ]
  • [ 3150-24-1 ]
  • N-acetyl-D-lactosamine [ No CAS ]
  • Gal-β[1→6]GlcNAc [ No CAS ]
  • [ 81573-30-0 ]
YieldReaction ConditionsOperation in experiment
1: 7 %Chromat. 2: 8 %Chromat. 3: 80 %Chromat. With 2-hydroxy-N,N-dimethyl-propanamide; Thermus thermophilus β-galactosidase In aq. phosphate buffer at 60℃; for 3h; Enzymatic reaction; regioselective reaction; Disaccharide synthesis General procedure: Transglycosylation reactions were carried out in 1.0 mL of solution (2 M solvent)-sodium phosphate buffer (50 mM, pH 6.0), with 51.2 mg (0.17 M) pNP-b-Gal (donor) and 188 g (0.85 M) of GlcNAc (acceptor) mixture was preequilibrated to 60 C. Afterwards, 36 mmol min 1 (U) of T. thermophilus b-galactosidase were added to the reaction mixture and reaction was incubated during 3 h, then, was stopped (and homogenized in the case of biphasic systems) by addition of methanol. Reaction yields were determined by HPLC-ELSD. The crude mixture was then directly loaded onto a carboneCelite column eluted with a linear gradient of 0e15% (v/v) of ethanol in water. Solvents were eliminated and disaccharide (LacNAc) was dissolved in D2O to be characterized by 1H and 13C NMR spectroscopy. NMR spectra for LacNAc were consistent to previous reports.
  • 78
  • N-Acetyl-D-glucosamine [ No CAS ]
  • [ 3150-24-1 ]
  • N-acetyl-D-lactosamine [ No CAS ]
  • Gal-β[1→6]GlcNAc [ No CAS ]
  • [ 80321-98-8 ]
YieldReaction ConditionsOperation in experiment
1: 17 %Chromat. 2: 6 %Chromat. 3: 77 %Chromat. With Thermus thermophilus β-galactosidase; 5-hydroxy-1,3-dioxan-2-one In aq. phosphate buffer at 60℃; for 3h; Enzymatic reaction; regioselective reaction; Disaccharide synthesis General procedure: Transglycosylation reactions were carried out in 1.0 mL of solution (2 M solvent)-sodium phosphate buffer (50 mM, pH 6.0), with 51.2 mg (0.17 M) pNP-b-Gal (donor) and 188 g (0.85 M) of GlcNAc (acceptor) mixture was preequilibrated to 60 C. Afterwards, 36 mmol min 1 (U) of T. thermophilus b-galactosidase were added to the reaction mixture and reaction was incubated during 3 h, then, was stopped (and homogenized in the case of biphasic systems) by addition of methanol. Reaction yields were determined by HPLC-ELSD. The crude mixture was then directly loaded onto a carboneCelite column eluted with a linear gradient of 0e15% (v/v) of ethanol in water. Solvents were eliminated and disaccharide (LacNAc) was dissolved in D2O to be characterized by 1H and 13C NMR spectroscopy. NMR spectra for LacNAc were consistent to previous reports.
  • 79
  • N-Acetyl-D-glucosamine [ No CAS ]
  • [ 3150-24-1 ]
  • N-acetyl-D-lactosamine [ No CAS ]
  • Gal-β[1→6]GlcNAc [ No CAS ]
YieldReaction ConditionsOperation in experiment
1: 15 %Chromat. 2: 75 %Chromat. With 1,3-dimethyl glycerol ether; Thermus thermophilus β-galactosidase In aq. phosphate buffer at 60℃; for 3h; Enzymatic reaction; regioselective reaction; Disaccharide synthesis General procedure: Transglycosylation reactions were carried out in 1.0 mL of solution (2 M solvent)-sodium phosphate buffer (50 mM, pH 6.0), with 51.2 mg (0.17 M) pNP-b-Gal (donor) and 188 g (0.85 M) of GlcNAc (acceptor) mixture was preequilibrated to 60 C. Afterwards, 36 mmol min 1 (U) of T. thermophilus b-galactosidase were added to the reaction mixture and reaction was incubated during 3 h, then, was stopped (and homogenized in the case of biphasic systems) by addition of methanol. Reaction yields were determined by HPLC-ELSD. The crude mixture was then directly loaded onto a carboneCelite column eluted with a linear gradient of 0e15% (v/v) of ethanol in water. Solvents were eliminated and disaccharide (LacNAc) was dissolved in D2O to be characterized by 1H and 13C NMR spectroscopy. NMR spectra for LacNAc were consistent to previous reports.
  • 80
  • [ 1226-39-7 ]
  • [ 35599-02-1 ]
  • [ 2106-10-7 ]
  • [ 2001-96-9 ]
  • [ 2492-87-7 ]
  • [ 3150-24-1 ]
  • 4-nitrophenyl β-D-glucopyranosyl-(1->3)-β-D-fucopyranoside [ No CAS ]
  • 4-nitrophenyl β-D-glucopyranosyl-(1->3)-β-D-galactopyranoside [ No CAS ]
  • C23H33NO17 [ No CAS ]
  • 4-nitrophenyl β-D-glucopyranosyl-(1->4)-β-D-xylopyranoside [ No CAS ]
  • [ 26255-70-9 ]
  • 4-nitrophenyl β-D-glucopyranosyl-(1->3)-β-D-xylopyranoside [ No CAS ]
  • 4-nitrophenyl β-D-glucopyranosyl-(1→4)-β-D-mannopyranoside [ No CAS ]
  • [ 2713-54-4 ]
  • 81
  • N-acetyl-D-galactosamine [ No CAS ]
  • [ 3150-24-1 ]
  • [ 20972-29-6 ]
YieldReaction ConditionsOperation in experiment
99% With 2-hydroxy-N,N-dimethyl-propanamide; β-galactosidase-3-N-terminal 6-histidine tag from Bacillus circulans ATCC 31382 In aq. phosphate buffer at 37 - 100℃; Green chemistry; Enzymatic reaction; regioselective reaction;
98% With β-GaL-3-NTag from B. circulans ATCC 31382; 3-butyl-1-methyl-1H-imidazol-3-ium hexafluorophosphate In aq. phosphate buffer at 37℃; for 3h; Enzymatic reaction; 4.4. Transgalactosylation reactions General procedure: pNP-β-Gal (85 mM) and GlcNAc or GalNAc (425 mM) were dissolved in 1.00 ml of buffer sodium phosphate 50 mM pH 6 and different percentages of ILs, and pre-warmed at reaction temperature (37 °C). Reaction started by addition of biocatalyst to the mixture: 5 U of recombinant enzyme. Aliquots (50 μl) were withdrawn from reaction media at different times. The reaction was stopped after 3 h by heating to 100 °C for 5 min and conserved immediately at -20 °C. Analytical determination of products were performed by HPLC using an NH2P50-4E amino column (Asahipak, Japan) using three detectors: ELSD (Evaporative Light Scattering), UV-vis at 317 nm and CD (Circular Dichroism). Each experimental assay was determined at least three times with standard deviation under 5% of the average of samples.
  • 82
  • N-acetyl-D-galactosamine [ No CAS ]
  • [ 3150-24-1 ]
  • [ 59-23-4 ]
  • [ 20972-29-6 ]
  • 2-acetamido-2-deoxy-6-O-β-D-galactopyranosyl-D-galactose [ No CAS ]
YieldReaction ConditionsOperation in experiment
1: 59% 2: 10% 3: 7% With β-GaL-3-NTag from B. circulans ATCC 31382; 1-butyl-3-methylimidazolium Tetrafluoroborate In aq. phosphate buffer at 37℃; for 3h; Enzymatic reaction; 4.4. Transgalactosylation reactions General procedure: pNP-β-Gal (85 mM) and GlcNAc or GalNAc (425 mM) were dissolved in 1.00 ml of buffer sodium phosphate 50 mM pH 6 and different percentages of ILs, and pre-warmed at reaction temperature (37 °C). Reaction started by addition of biocatalyst to the mixture: 5 U of recombinant enzyme. Aliquots (50 μl) were withdrawn from reaction media at different times. The reaction was stopped after 3 h by heating to 100 °C for 5 min and conserved immediately at -20 °C. Analytical determination of products were performed by HPLC using an NH2P50-4E amino column (Asahipak, Japan) using three detectors: ELSD (Evaporative Light Scattering), UV-vis at 317 nm and CD (Circular Dichroism). Each experimental assay was determined at least three times with standard deviation under 5% of the average of samples.
1: 50% 2: 42% 3: 8% With β-GaL-3-NTag from B. circulans ATCC 31382; water; 1-butyl-3-methylimidazolium trifluoromethanesulfonimide In aq. phosphate buffer at 37℃; for 3h; Enzymatic reaction; 4.4. Transgalactosylation reactions General procedure: pNP-β-Gal (85 mM) and GlcNAc or GalNAc (425 mM) were dissolved in 1.00 ml of buffer sodium phosphate 50 mM pH 6 and different percentages of ILs, and pre-warmed at reaction temperature (37 °C). Reaction started by addition of biocatalyst to the mixture: 5 U of recombinant enzyme. Aliquots (50 μl) were withdrawn from reaction media at different times. The reaction was stopped after 3 h by heating to 100 °C for 5 min and conserved immediately at -20 °C. Analytical determination of products were performed by HPLC using an NH2P50-4E amino column (Asahipak, Japan) using three detectors: ELSD (Evaporative Light Scattering), UV-vis at 317 nm and CD (Circular Dichroism). Each experimental assay was determined at least three times with standard deviation under 5% of the average of samples.
1: 45% 2: 32% 3: 23% With β-GaL-3-NTag from B. circulans ATCC 31382; cocosalkylpentaethoxymethylammonium methylsulfate; water In aq. phosphate buffer at 37℃; for 3h; Enzymatic reaction; 4.4. Transgalactosylation reactions General procedure: pNP-β-Gal (85 mM) and GlcNAc or GalNAc (425 mM) were dissolved in 1.00 ml of buffer sodium phosphate 50 mM pH 6 and different percentages of ILs, and pre-warmed at reaction temperature (37 °C). Reaction started by addition of biocatalyst to the mixture: 5 U of recombinant enzyme. Aliquots (50 μl) were withdrawn from reaction media at different times. The reaction was stopped after 3 h by heating to 100 °C for 5 min and conserved immediately at -20 °C. Analytical determination of products were performed by HPLC using an NH2P50-4E amino column (Asahipak, Japan) using three detectors: ELSD (Evaporative Light Scattering), UV-vis at 317 nm and CD (Circular Dichroism). Each experimental assay was determined at least three times with standard deviation under 5% of the average of samples.
  • 83
  • [ 72-87-7 ]
  • [ 3150-24-1 ]
  • [ 59-23-4 ]
  • [ 20972-29-6 ]
YieldReaction ConditionsOperation in experiment
9%; 91% With beta-GaL-3-NTag from B. circulans ATCC 31382; water; methyltrioctylammonium bistriflamide; In aq. phosphate buffer; at 37℃; for 3h;pH 6.0;Enzymatic reaction; General procedure: pNP-beta-Gal (85 mM) and GlcNAc or GalNAc (425 mM) were dissolved in 1.00 ml of buffer sodium phosphate 50 mM pH 6 and different percentages of ILs, and pre-warmed at reaction temperature (37 C). Reaction started by addition of biocatalyst to the mixture: 5 U of recombinant enzyme. Aliquots (50 mul) were withdrawn from reaction media at different times. The reaction was stopped after 3 h by heating to 100 C for 5 min and conserved immediately at -20 C. Analytical determination of products were performed by HPLC using an NH2P50-4E amino column (Asahipak, Japan) using three detectors: ELSD (Evaporative Light Scattering), UV-vis at 317 nm and CD (Circular Dichroism). Each experimental assay was determined at least three times with standard deviation under 5% of the average of samples.
78%; 22% With beta-GaL-3-NTag from B. circulans ATCC 31382; water; 1-butyl-3-methylimidazolium methylsulfate; In aq. phosphate buffer; at 37℃; for 3h;pH 6.0;Enzymatic reaction; General procedure: pNP-beta-Gal (85 mM) and GlcNAc or GalNAc (425 mM) were dissolved in 1.00 ml of buffer sodium phosphate 50 mM pH 6 and different percentages of ILs, and pre-warmed at reaction temperature (37 C). Reaction started by addition of biocatalyst to the mixture: 5 U of recombinant enzyme. Aliquots (50 mul) were withdrawn from reaction media at different times. The reaction was stopped after 3 h by heating to 100 C for 5 min and conserved immediately at -20 C. Analytical determination of products were performed by HPLC using an NH2P50-4E amino column (Asahipak, Japan) using three detectors: ELSD (Evaporative Light Scattering), UV-vis at 317 nm and CD (Circular Dichroism). Each experimental assay was determined at least three times with standard deviation under 5% of the average of samples.
  • 84
  • N-Acetyl-D-glucosamine [ No CAS ]
  • [ 3150-24-1 ]
  • 2-Acetamido-2-deoxy-6-O-(β-D-galactopyranosyl)-D-glucose [ No CAS ]
  • lacto-N-biose [ No CAS ]
  • [ 59-23-4 ]
YieldReaction ConditionsOperation in experiment
1: 53% 2: 33% 3: 15% With β-GaL-3-NTag from B. circulans ATCC 31382; cocosalkylpentaethoxymethylammonium methylsulfate; water In aq. phosphate buffer at 37℃; for 3h; Enzymatic reaction; 4.4. Transgalactosylation reactions General procedure: pNP-β-Gal (85 mM) and GlcNAc or GalNAc (425 mM) were dissolved in 1.00 ml of buffer sodium phosphate 50 mM pH 6 and different percentages of ILs, and pre-warmed at reaction temperature (37 °C). Reaction started by addition of biocatalyst to the mixture: 5 U of recombinant enzyme. Aliquots (50 μl) were withdrawn from reaction media at different times. The reaction was stopped after 3 h by heating to 100 °C for 5 min and conserved immediately at -20 °C. Analytical determination of products were performed by HPLC using an NH2P50-4E amino column (Asahipak, Japan) using three detectors: ELSD (Evaporative Light Scattering), UV-vis at 317 nm and CD (Circular Dichroism). Each experimental assay was determined at least three times with standard deviation under 5% of the average of samples.
1: 44% 2: 37% 3: 19% With β-GaL-3-NTag from B. circulans ATCC 31382; water; 1-hexyl-3-methylimidazolium bis-(trifluoromethanesulfonyl)amide In aq. phosphate buffer at 37℃; for 3h; Enzymatic reaction; 4.4. Transgalactosylation reactions General procedure: pNP-β-Gal (85 mM) and GlcNAc or GalNAc (425 mM) were dissolved in 1.00 ml of buffer sodium phosphate 50 mM pH 6 and different percentages of ILs, and pre-warmed at reaction temperature (37 °C). Reaction started by addition of biocatalyst to the mixture: 5 U of recombinant enzyme. Aliquots (50 μl) were withdrawn from reaction media at different times. The reaction was stopped after 3 h by heating to 100 °C for 5 min and conserved immediately at -20 °C. Analytical determination of products were performed by HPLC using an NH2P50-4E amino column (Asahipak, Japan) using three detectors: ELSD (Evaporative Light Scattering), UV-vis at 317 nm and CD (Circular Dichroism). Each experimental assay was determined at least three times with standard deviation under 5% of the average of samples.
1: 43% 2: 41% 3: 16% With β-GaL-3-NTag from B. circulans ATCC 31382; water; 1-octyl-3-methylimidazolium hexafluorophosphate In aq. phosphate buffer at 37℃; for 3h; Enzymatic reaction; 4.4. Transgalactosylation reactions General procedure: pNP-β-Gal (85 mM) and GlcNAc or GalNAc (425 mM) were dissolved in 1.00 ml of buffer sodium phosphate 50 mM pH 6 and different percentages of ILs, and pre-warmed at reaction temperature (37 °C). Reaction started by addition of biocatalyst to the mixture: 5 U of recombinant enzyme. Aliquots (50 μl) were withdrawn from reaction media at different times. The reaction was stopped after 3 h by heating to 100 °C for 5 min and conserved immediately at -20 °C. Analytical determination of products were performed by HPLC using an NH2P50-4E amino column (Asahipak, Japan) using three detectors: ELSD (Evaporative Light Scattering), UV-vis at 317 nm and CD (Circular Dichroism). Each experimental assay was determined at least three times with standard deviation under 5% of the average of samples.
  • 85
  • [ 7512-17-6 ]
  • [ 3150-24-1 ]
  • [ 489-52-1 ]
  • [ 59-23-4 ]
YieldReaction ConditionsOperation in experiment
88%; 12% With beta-GaL-3-NTag from B. circulans ATCC 31382; water; methyltrioctylammonium bistriflamide; In aq. phosphate buffer; at 37℃; for 3h;pH 6.0;Enzymatic reaction; General procedure: pNP-beta-Gal (85 mM) and GlcNAc or GalNAc (425 mM) were dissolved in 1.00 ml of buffer sodium phosphate 50 mM pH 6 and different percentages of ILs, and pre-warmed at reaction temperature (37 C). Reaction started by addition of biocatalyst to the mixture: 5 U of recombinant enzyme. Aliquots (50 mul) were withdrawn from reaction media at different times. The reaction was stopped after 3 h by heating to 100 C for 5 min and conserved immediately at -20 C. Analytical determination of products were performed by HPLC using an NH2P50-4E amino column (Asahipak, Japan) using three detectors: ELSD (Evaporative Light Scattering), UV-vis at 317 nm and CD (Circular Dichroism). Each experimental assay was determined at least three times with standard deviation under 5% of the average of samples.
20%; 80% With beta-GaL-3-NTag from B. circulans ATCC 31382; water; 1-butyl-3-methylimidazolium methylsulfate; In aq. phosphate buffer; at 37℃; for 3h;pH 6.0;Enzymatic reaction; General procedure: pNP-beta-Gal (85 mM) and GlcNAc or GalNAc (425 mM) were dissolved in 1.00 ml of buffer sodium phosphate 50 mM pH 6 and different percentages of ILs, and pre-warmed at reaction temperature (37 C). Reaction started by addition of biocatalyst to the mixture: 5 U of recombinant enzyme. Aliquots (50 mul) were withdrawn from reaction media at different times. The reaction was stopped after 3 h by heating to 100 C for 5 min and conserved immediately at -20 C. Analytical determination of products were performed by HPLC using an NH2P50-4E amino column (Asahipak, Japan) using three detectors: ELSD (Evaporative Light Scattering), UV-vis at 317 nm and CD (Circular Dichroism). Each experimental assay was determined at least three times with standard deviation under 5% of the average of samples.
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