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

Description

P-NITROPHENYL BETA-D-N,N',N''-TRIACETYLCHITOTRIOSE is a solid chemical compound that serves as a substrate for the hydrolytic activity of chitinase enzyme. It is characterized by the release of a chromogenic end product, p-nitrophenol, which can be measured at 405 nm. P-NITROPHENYL BETA-D-N,N',N''-TRIACETYLCHITOTRIOSE is particularly useful in the determination of endochitinase activity in various proteins and enzymes.

Uses

1. Used in Enzyme Activity Analysis:
P-NITROPHENYL BETA-D-N,N',N''-TRIACETYLCHITOTRIOSE is used as a substrate for analyzing the enzyme activity of chitinases, specifically for determining the endochitinase activity of novel proteins and enzymes. This application is crucial in understanding the functionality and efficiency of these enzymes in various biological processes.
2. Used in Agricultural and Biological Research:
In the field of agricultural and biological research, P-NITROPHENYL BETA-D-N,N',N''-TRIACETYLCHITOTRIOSE is used as a tool to study the chitinase enzyme's role in plant defense mechanisms and its potential applications in pest control and disease resistance.
3. Used in Pharmaceutical and Biotechnology Industries:
P-NITROPHENYL BETA-D-N,N',N''-TRIACETYLCHITOTRIOSE is used as a reagent in the pharmaceutical and biotechnology industries for the development and optimization of chitinase-based drugs and therapies. Its ability to act as a substrate for chitinase enzyme activity makes it a valuable asset in the research and development of novel treatments for various diseases and conditions.
4. Used in Quality Control and Diagnostics:
In the quality control and diagnostics sector, P-NITROPHENYL BETA-D-N,N',N''-TRIACETYLCHITOTRIOSE is employed as a reference material to ensure the accuracy and reliability of chitinase enzyme activity assays. This helps in the standardization of test procedures and the development of more accurate diagnostic tools.

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,