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Characterization of Chitinase Produced by the Alkaliphilic Bacillus mannanilyticus IB-OR17 B1 Strain

Characterization of Chitinase Produced by the Alkaliphilic Bacillus mannanilyticus IB-OR17 B1 Strain The paper reports on the isolation of an extracellular chitinase produced by the alkaliphilic Bacillus mannanilyticus IB-OR17 B1 strain grown in media containing crab shell and bee chitin at a pH of 8–11. The enzyme was 860-fold purified by ultrafiltration and chitin sorption. The molecular weight of the purified chitinase was shown by denaturing electrophoresis to be 56 kDa. The enzyme showed maximum activity at a pH of 7.5–8.0 and 65°C and was stable within a pH range of 3.5–10.5 and temperature range of 75–85°C. With colloidal chitin as substrate, the kinetic characteristics of the chitinase were determined as follows: K M ~ 1.32 mg/mL and V max ~ 5.05 μM min–1. N-acetyl-D-glucosamine and its dimer were the main products of enzymatic chitin cleavage, while the trisaccharide was detected just in minor quantities. The chitinase actively hydrolyzed p-nitrophenyl-GlcNAc2 according to the exo-mechanism of substrate hydrolysis characteristic of chitobiosidases. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Microbiology Springer Journals

Characterization of Chitinase Produced by the Alkaliphilic Bacillus mannanilyticus IB-OR17 B1 Strain

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References (1)

Publisher
Springer Journals
Copyright
Copyright © 2018 by Pleiades Publishing, Inc.
Subject
Life Sciences; Biochemistry, general; Microbiology; Medical Microbiology
ISSN
0003-6838
eISSN
1608-3024
DOI
10.1134/S0003683818050022
Publisher site
See Article on Publisher Site

Abstract

The paper reports on the isolation of an extracellular chitinase produced by the alkaliphilic Bacillus mannanilyticus IB-OR17 B1 strain grown in media containing crab shell and bee chitin at a pH of 8–11. The enzyme was 860-fold purified by ultrafiltration and chitin sorption. The molecular weight of the purified chitinase was shown by denaturing electrophoresis to be 56 kDa. The enzyme showed maximum activity at a pH of 7.5–8.0 and 65°C and was stable within a pH range of 3.5–10.5 and temperature range of 75–85°C. With colloidal chitin as substrate, the kinetic characteristics of the chitinase were determined as follows: K M ~ 1.32 mg/mL and V max ~ 5.05 μM min–1. N-acetyl-D-glucosamine and its dimer were the main products of enzymatic chitin cleavage, while the trisaccharide was detected just in minor quantities. The chitinase actively hydrolyzed p-nitrophenyl-GlcNAc2 according to the exo-mechanism of substrate hydrolysis characteristic of chitobiosidases.

Journal

Applied Biochemistry and Microbiology – Springer Journals

Published: Sep 14, 2018

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