38864-21-0

Basic information

• Product Name: N,N',N''-TRIACETYLCHITOTRIOSE
• Synonyms: Tri(N-acetylglucosaMine);GlcNAcβ(1-4)GlcNAcβ(1-4)GlcNAc;N-acetylated Chitotriose;N,N',N''-TRIACETYLCHITOTRIOSE;N,N',N'-TRIACETYLCHITOTRIOSE;O-[2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSYL-(1->4)]-O-[2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYR-ANOSYL-(1->4)]-2-ACETAMIDO-2-DEOXY-D-GLUCOPYRANOSE;CHITOTRIOSE;CHITOTRIOSE, TRI-N-ACETYL
• CAS NO: 38864-21-0
• Molecular Formula: C₂₄H₄₁N₃O₁₆
• Molecular Weight: 627.59
• Product Categories: Oligosaccharides
• Mol File: 38864-21-0.mol
• Article Data: 1

Chemical Properties

• Melting Point: 271-272°C dec.
• Boiling Point: 1146.9 °C at 760 mmHg
• Flash Point: 647.4 °C
• Appearance: /
• Density: 1.54 g/cm3
• Storage Temp.: −20°C
• Solubility: H2O: 50 mg/mL, clear to slightly hazy, colorless to faintly
• PKA: 12.72±0.70(Predicted)
• BRN: 75249
• CAS DataBase Reference: N,N',N''-TRIACETYLCHITOTRIOSE(CAS DataBase Reference)
• NIST Chemistry Reference: N,N',N''-TRIACETYLCHITOTRIOSE(38864-21-0)
• EPA Substance Registry System: N,N',N''-TRIACETYLCHITOTRIOSE(38864-21-0)

Safety Data

• Safety Statements: 24/25
• WGK Germany: 3
• F: 10-21
• Hazardous Substances Data: 38864-21-0(Hazardous Substances Data)

Usage

Description

N,N',N''-TRIACETYLCHITOTRIOSE is a triose oligosaccharide derived from chitin, consisting of three N-acetylglucosamine units. It possesses the ability to scavenge reactive oxygen species and protect DNA from oxidative damage.

Uses

Used in Antioxidant Applications:
N,N',N''-TRIACETYLCHITOTRIOSE is used as an antioxidant agent for its ability to scavenge reactive oxygen species and protect DNA from oxidative damage.
Used in Pharmaceutical Industry:
N,N',N''-TRIACETYLCHITOTRIOSE is used as a specific coagulant for its strong crosslinking activity with lectins, making it a valuable component in the development of pharmaceutical products.

Reactions

The hydrolytic activity of lysozyme towards 4-methylumbelliferyl tetra-N-acetyl-β-chitotetraoside (4-MU-(GlcNAc)4) was little affected by ionic strength, though the activity of lysozyme towards cell suspension of Micrococcus lysodeikticus varied markedly with ionic strength. About 40-60percent of lysozyme activity with 4-MU-(GlcNAc)4 as a substrate was inhibited by 0.1 mM N,N',N''-triacetylchitotriose ((GlcNAc)3), but the lytic activity of lysozyme towards M. lysodeikticus was little affected. The kinetics of hydrolysis of 4-MU-(GlcNAc)4 by hen eggwhite (HEW) lysozyme and human placental (HP) lysozyme and the inhibition of this hydrolysis by (GlcNAc)3 were investigated. The K(s) values for 4-MU-(GlcNAc)4 of HEW- and HP-lysozymes were 19.7 and 27.9 μM, respectively, and the V(max) values were 0.124 and 0.0833 nmol/min/mg, respectively. The k values of both enzymes were very low, implying a poor orientation of the scissile bond in the substrate molecule with respect to the active site of lysozyme. (GlcNAc)3 inhibited lysozyme with hyperbolic mixed-type inhibition. The inhibition reduced V(max) values of both lysozymes. The K(s) value of HEW-lysozyme was increased by the addition of the inhibitory whereas the K(s) value of HP-lysozyme was decreased. The K(i) value was 29.6 μm for HEW-lysozyme and 106 μM for HP-lysozyme. Hydrolysis of 4-methylumbelliferyl tetra-N-acetyl-β-chitotetraoside by lysozyme and its inhibition by N,N',N''-triacetylchitotriose Tanimoto; Fukuda; Kawamura - Chemical and Pharmaceutical Bulletin, 1984, vol. 32, # 9, p. 3607 - 361

Relevant articles and documents

Process optimization, purification and characterization of a novel acidic, thermostable chitinase from Humicola grisea

An extracellular acidic and thermostable chitinase (HgChi) from thermophilic Humicola grisea was purified and characterized. Enhancement in chitinase production (Qp = 2.9662 Ul?1 h?1) was achieved through derivation of optimum fermentation conditions via central composite design. H. grisea observed to produce various isoforms of chitinase, among which the major expressed form has molecular mass of about 50 kDa. Purified chitinases exhibited optimal activity at pH 3.0 and 70 °C. Chitinase showed notable stability at increasing temperatures. Half-life of chitinase is 169.06 min at optimum temperature. Chitinase has effectively catalyzed N-acetyl chitobiose (GlcNAc)2, and N-acetyl chitotriose (GlcNAc)3 and colloidal chitin. Purified chitinase from H. grisea showed high affinity towards colloidal chitin as evident by its comparatively lower Km value. Presence of metal ions viz. Mn2+, Co2+, NH4 + and Mg2+ significantly increased the chitinase activity. Thin layer chromatography (TLC) analysis revealed the significant hydrolyzing competence of HgChi for colloidal chitin, (GlcNAc)3 and (GlcNAc)2 into oligomers and N-acetyl–D-glucosamine (GlcNAc). Thermostable chitinase appeared as potential candidate for efficient conversion of chitin to bioactive oligosaccharides at industrial scale.