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Usage

Uses

Used in Pharmaceutical Industry:
N,N'-Diacetylchitobiose is used as an inhibitor of lysozyme, which is an enzyme that breaks down the cell walls of bacteria. This application is particularly useful in the treatment of Escherichia coli sepsis in dogs, as it helps reverse myocardial depression and lessens norepinephrine requirements.
Used in Immunology Research:
As a lectin inhibitor and immunopotentiator, N,N'-Diacetylchitobiose plays a crucial role in the study of the immune system. It helps researchers understand the interactions between lectins and other molecules, which can lead to the development of new therapies for various immune-related conditions.
Used in Microbiology and Fermentation Research:
N,N'-Diacetylchitobiose is used as an alternative source of N-acetylglucosamine by some bacteria. It is particularly useful in fermentation research, where it helps scientists study, differentiate, and characterize chitobiose transporter systems and enzymes such as β-N-acetylglucosaminidase(s) and chitobiose phosphorylase(s). This knowledge can be applied to improve the efficiency of fermentation processes and the production of various biotechnological products.

Biochem/physiol Actions

In chitinolytic bacteria, such as Vibrio, Streptomyces and Serratia, N,N′-Diacetylchitobiose (GlcNAc2) is not only a major breakdown product of chitinase, but it is also the smallest substance that induces chitinase production. It can also be utilized as a carbon source by E. coli, which does not express chitinases, but is exposed to GlcNAc2 produced by intestinal chitinolytic bacteria. In most organisms, the uptake of GlcNAc2 occurs via the phosphoenolpyruvate:glycose phosphotransferase system (PTS). GlcNAc2 has also been used as a substrate or inhibitor to study the activity of glycolytic enzymes.

Purification Methods

Recrystallise N,N'-Diacetylchitobiose from aqueous MeOH or aqueous EtOH/1,2-dimethoxyethane. [Zilliken et al. J Chem Soc 77 1296 1955, Beilstein 18/11 V 147.]

Upstream product

• 1398-61-4 chitin 

Relevant academic research and scientific papers

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.

Cloning and expression of chitinase a from serratia marcescens for large-scale preparation of N,N-Diacetyl chitobiose

The gene of Serratia marcescens chitinase A(chiA) was cloned by PCR. The complete gene was constructed into a pRSET vector and expressed in Escherichia coli. The recombinant enzyme was purified to > 90% homogeneity by hydrophobic interaction chromatograph