139639-82-0

Basic information

• Product Name: o-nitrophenyl β-D-galactopyranosyl<1->3>-β-D-galactopyranoside
• Synonyms: o-nitrophenyl β-D-galactopyranosyl<1->3>-β-D-galactopyranoside
• CAS NO: 139639-82-0
• Molecular Weight: 463.395
• Mol File: 139639-82-0.mol

Chemical Properties

• CAS DataBase Reference: o-nitrophenyl β-D-galactopyranosyl<1->3>-β-D-galactopyranoside(CAS DataBase Reference)
• NIST Chemistry Reference: o-nitrophenyl β-D-galactopyranosyl<1->3>-β-D-galactopyranoside(139639-82-0)
• EPA Substance Registry System: o-nitrophenyl β-D-galactopyranosyl<1->3>-β-D-galactopyranoside(139639-82-0)

Safety Data

• Hazardous Substances Data: 139639-82-0(Hazardous Substances Data)

Upstream product

• 2816-24-2 o-nitrophenyl D-galactopyranoside 
• 97-30-3 methyl-alpha-D-glucopyranoside 
• 3396-99-4 methyl α-D-galactopyranoside 

Relevant articles and documents

Galactosylation and glucosylation by use of β-galactosidase

The transglucosylation activity of β-galactosidase derived from Aspergillus oryzae and Escherichia coli, respectively, was examined in reaction systems containing up to 50% acetonitrile. Starting with ortho-nitrophenyl β-galactoside (1), which functions both as donor and as acceptor, β-Gal(1-6)β-Gal-PhNO2-o (2) and β-Gal(1-3)β-Gal-PhNO2-o (3) were obtained. Under similar conditions the enzyme from A. oryzae converts para-nitrophenyl β-glucoside (5) to β-Glc(1-2)β-Glc-PhNO2-p (6) and α-Glc(1-4)β-Glc-PhNO2-p (7). Incubation of 1 and L-serine in the presence of the A. oryzae β-galactosidase leads to β-Gal-L-Ser (4).

Enzymatic syntheses and selective hydrolysis of O-β-d- galactopyranosides using a marine mollusc β-galactosidase

The use of crude extract of the hepatopancreas of Aplysia fasciata, a large mollusc belonging to the order Anaspidea containing a β-galactosidase activity, was reported for the synthesis of different galactosides. Good yields with polar acceptors and the

Probing the transferase activity of glycosidases by means of in situ NMR spectroscopy

This paper describes the conditions in which in situ NMR spectroscopy is a suitable technique to use when following the course of enzymatic transglycosylation reactions. Using this methodology, the reactions must be carried out in D2O. Our experiments indicate that the rate of the transglycosylation reaction is reduced in this solvent while the rate of the hydrolysis of the disaccharides produced is enhanced depending on the nature of the anomeric substituent. However, this undesirable effect is generally weak because the rates of the transglycosylation reactions are always faster than the rates of the hydrolysis whatever the solvent. The great advantage of NMR spectroscopy lies in its potential to detect, in a single experiment, all the components of the reaction without any disturbance of the reaction medium.

Transferase activity of a β-glycosidase from Thermus thermophilus: Specificities and limits - Application to the synthesis of β-[1 → 3]- disaccharides

The aim of this paper is to test the ability of a β-glycosidase from Thermus thermophilus to catalyse transglycosylation reactions in the presence of nitrophenyl glycosides as donors and other monosaccharides as acceptors. Our results show that this enzym