80321-98-8

Upstream product

• 3767-28-0 4-nitrophenyl-α-D-glucopyranoside 
• 62847-72-7 4-nitrophenyl 2,3-di-O-acetyl-β-D-galactopyranoside 
• 108-24-7 acetic anhydride 
• 2816-24-2 o-nitrophenyl D-galactopyranoside 
• 3150-24-1 4-nitrophenyl-β-D-galactopyranoside 
• 102717-07-7 p-nitrophenyl 2,3,4-tri-O-benzoyl-β-D-galactopyranoside 
• 2492-87-7 p-nitrophenyl β-D-mannopyranoside 
• 7512-17-6 N-Acetyl-D-glucosamine 
• 64970-96-3 p-nitrophenyl 4,6-O-isopropylidene-β-D-galactopyranoside 
• 102717-06-6 C₅₂H₄₁NO₁₁ 
• 102717-05-5 p-nitrophenyl 6-O-trityl-β-D-galactopyranoside 
• 61198-88-7 2,3,4,6-tetra-O-benzoyl-α-D-galactopyranosyl bromide 
• 102717-08-8 p-nitrophenyl O-(2,3,4,6-tetra-O-benzoyl-β-D-galactopyranosyl)-(1-6)-2,3,4-tri-O-benzoyl-β-D-galactopyranoside 
• 80321-97-7 p-nitrophenyl 6-O-β-D-galactopyranosyl-3,4-O-isopropylidene-β-D-galactopyranoside 

Downstream Products

• 80373-95-1 p-nitrophenyl 2,3,4-tri-O-acetyl-6-O-(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-β-D-galactopyranoside 

Relevant academic research and scientific papers

Optimised N-acetyl-D-lactosamine synthesis using Thermus thermophilus β-galactosidase in bio-solvents

Synthesis of N-acetyl-D-lactosamine (Gal-β[1→4]GlcNAc, LacNAc) catalyzed by β-galactosidase from Thermus thermophilus (TTP0042) is affected by side reactions that give as result very low yields (about 20%) of LAcNAc when the reaction is performed in buffer. The process is improved (up to 91% of disaccharide yield) when the reaction takes place in the presence of solvents from biomass (bio-solvents) at 2.0 M concentration. Most of the solvents tested increased the LacNAc synthesis and reduced the undesired side reactions. In order to understand the possible effects of these solvents over the enzyme regioselectivity, we developed a conformational study of the enzyme structure in the presence of a selected bio-solvent by circular dichroism and fluorescence. According to this study, we were able to conclude that the presence of bio-solvents in the reaction media modifies the enzyme secondary and tertiary structure and this may be the cause of the regioselectivity changes observed in the transglycosylation reaction.

Isolation and characterization of a novel α-glucosidase with transglycosylation activity from Arthrobacter sp. DL001

A strain of Arthrobacter sp. DL001 with high transglycosylation activity was successfully isolated from the Yellow Sea of China. To purify the extracellular enzyme responsible for transglycosylation, a four-step protocol was adopted and the enzyme with electrophoretical purity was obtained. The purified enzyme has a molecular mass of 210 kDa and displays a narrow hydrolysis specificity towards α-1,4-glucosidic bond. Its hydrolytic activity was identified as decreasing in the order of maltotriose > panose > maltose. Only 3.61% maltose activity occurs when p-nitrophenyl α-d-glycopyranoside serves as a substrate, suggesting that this enzyme belongs to the type II α-glucosidase. In addition, the enzyme was able to transfer glucosyl groups from the donors containing α-1,4-glucosidic bond specific to glucosides, xylosides and alkyl alcohols in α-1,4- or α-1,6-manners. A decreased order of activity was observed when maltose, maltotriose, panose, β-cyclodextrin and soluble starch served as glycosyl donors, respectively. When maltose was utilized as a donor and a series of p-nitrophenyl-glycosides as acceptors, the glucosidase was capable of transferring glucosyl groups to p-nitrophenyl-glucosides and p-nitrophenyl-xylosides in α-1,4- or α-1,6-manners. The yields of p-nitrophenyl-oligosaccharides could reach 42-60% in 2 h. When a series of alkyl alcohols were utilized as acceptors, the enzyme exhibited its transglycosylation activities not only to the primary alcohols but also to the secondary alcohols with carbon chain length 1-4. Therefore, all the results indicated that the purified α-glucosidase present a useful tool for the biosynthesis of oligosaccharides and alkyl glucosides.

α-Glucosidase mutant catalyzes "α-glycosynthase"-type reaction

Replacement of the catalytic nucleophile Asp481 by glycine in Schizosaccharomyces pombe α-glucosidase eliminated the hydrolytic activity. The mutant enzyme (D481G) was found to catalyze the formation of an α-glucosidic linkage from β-glucosyl fluoride and

Regioselective synthesis of p-nitrophenyl glycosides of β-D-galactopyranosyl-disaccharides by transglycosylation with β-D-galactosidases

The β-D-galactosidase from porcine liver induced regiospecific transglycosylation of β-D-galactose from β-D-Gal-OC6H4NO2-o to OH-6 of, respectively, p-nitrophenyl glycoside acceptors of Gal, GlcNAc and GalNAc to afford β-G

SYNTHESIS OF p-NITROPHENYL β-GLYCOSIDES OF (1->6)-β-D-GALACTOPYRANOSYL-OLIGOSACCHARIDES

Sequential tritylation, benzoylation, and detritylation of p-nitrophenyl β-D-galactopyranoside gave p-nitrophenyl 2,3,4-tri-O-benzoyl-β-D-galactopyranoside (2).Reaction of 2 with 2,3,4,6-tetra-O-benzoyl-α-D-galactopyranosyl bromide gave p-nitrophenyl O-(2

ACETAL MIGRATION DURING GLYCOSYLATIONS CATALYZED BY MERCURIC CYANIDE: SYNTHESIS OF p-NITROPHENYL 6-O-β-D-GALACTOPYRANOSYL-β-D-GALACTOPYRANOSIDE

Isopropylidenation of p-nitrophenyl β-D-galactopyranoside under kinetic control afforded the 4,6-acetal (2).The structure of 2 was established by 1H- and 13C- n.m.r. spectroscopy, and confirmed by methylation, and hydrolysis to 2,3-di-O-methyl-D-galactose