7699-38-9

Basic information

• Product Name: P-NITROPHENYL BETA-D-N,N',N''-TRIACETYLCHITOTRIOSE
• Synonyms: P-NITROPHENYL BETA-D-N,N',N''-TRIACETYLCHITOTRIOSE;P-nitrophenyl B-D-N,N',N"-triacetyl*chitotriose;P-NITROPHENYL B-D-N,N',N"-TRIACETYL*CHIT OTRIOSE;4-nitrophenyl β-d-n,n',n''-triacetylchitotriose;4-NitrophenylN,N′,N′′-triacetyl-b-D-chitotriose;4-Nitrophenyl N,N',N''-triacetyl-β-D-chitotriose;(4-Nitrophenyl)-N,N',N'' -triacetyl-β-D-chitotrioside
• CAS NO: 7699-38-9
• Molecular Formula: C₃₀H₄₄N₄O₁₈
• Molecular Weight: 748.69
• EINECS: 1533716-785-6
• Product Categories: Chitobioside;ChromogenicEnzyme Substrates;Lysozyme;Substrates;Substrates by Enzyme
• Mol File: 7699-38-9.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 1184.8oC at 760 mmHg
• Flash Point: 670.3oC
• Appearance: /
• Density: 1.58g/cm3
• Storage Temp.: 2-8°C
• CAS DataBase Reference: P-NITROPHENYL BETA-D-N,N',N''-TRIACETYLCHITOTRIOSE(CAS DataBase Reference)
• NIST Chemistry Reference: P-NITROPHENYL BETA-D-N,N',N''-TRIACETYLCHITOTRIOSE(7699-38-9)
• EPA Substance Registry System: P-NITROPHENYL BETA-D-N,N',N''-TRIACETYLCHITOTRIOSE(7699-38-9)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 7699-38-9(Hazardous Substances Data)

Usage

Chemical Properties

solid

Uses

4-Nitrophenyl β-D-N,N′,N′′-triacetylchitotriose has been used as a substrate for determining the endochitinase activity of a novel protein isolated from the yam (Dioscorea opposita Thunb.) (DOI), enzyme activity of recombinant chitinase CvChi45.

General Description

4-Nitrophenyl β-D-N,N′,N′′-triacetylchitotriose is a substrate for hydrolytic activity of chitinase enzyme, with the release of chromogenic end product p-nitrophenol, measured at 405 nm.

Upstream product

• 3459-18-5 4-nitrophenyl N-acetyl-β-D-glucosaminide 
• 114882-45-0 p-Nitrophenyl penta-N-acetyl-β-chitopentaoside 

Relevant articles and documents

How Site-Directed Mutagenesis Boosted Selectivity of a Promiscuous Enzyme

β-N-Acetylhexosaminidases (GH20; EC 3.2.1.52) are exo-glycosidases with a dual activity for cleaving both N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) units from glycostructures. This substrate promiscuity is a hurdle in the selective synthesis of N-acetylhexosamine oligosaccharides combining both GlcNAc and GalNAc units since there are hardly any GalNAc transferring enzymes available for synthetic applications. We present here site-directed mutagenesis of a synthetically potent promiscuous β-N-acetylhexosaminidase from Talaromyces flavus (TfHex), which, as a wild type, exhibits a GalNAcase/GlcNAcase ratio of 1.2. On the basis of molecular modeling, we identified crucial amino acid residues responsible for its GalNAcase/GlcNAcase selectivity. Six site-directed mutants were prepared, heterologously expressed in Pichia pastoris, purified, and kinetically characterized. As a result, novel engineered enzymes with an up to 7-times higher selectivity for either GalNAc or GlcNAc substrates were obtained, preserving the favorable properties of the wild type TfHex, mainly its transglycosylation potential and tolerance to functional groups in the substrate molecule. The substrate selectivity and transglycosylation yield were further corroborated by reaction engineering. The new selective and synthetically capable enzymes were applied in the preparation of tailored N-acetylhexosamines. (Figure presented.).

Properties and Transglycosylation Reaction of a Chitinase from Nocardia orientalis

The hydrolytic products of a chitinase purified from Nocardia orientalis were examined on reduced (GlcNAc)n (n=2-6).The rate of hydrolysis on reduced (GlcNAc)4-6 increased with increasing chain-length of N-acetylglucosamine residues,