Isolation and characterization of the chitinase from Trichoderma asperellum

 Summary: Chitinases, a group of enzymes capable of degrading chitin directly to low molecular weight products, have been shown to be produced by a number of numerous bacteria, fungi, insects, plants, and animals. A chitinase producing strain was isolated from Thua Thien Hue, it was identified as Trichoderma asperellum SH16 using ITS sequence. Maximum activity of extracellular chitinase was observed after 96 h inoculation of micelia on 1% coloidal chitin medium. SDS - PAGE and native PAGE shown that molecular weight of this enzyme was 42 kDa and named as CHIT42-SH16. Characterization of the chitinase displayed an optimum pH at 7 and temperature at 40oC. The enzyme is stable between pH 3 - 9 and is able to retain its activity from 10 to 60oC. The presence of Al3+, Fe2+ and Ca2+ ions increased the CHIT42-SH16 activity up to 161%, 131%, and 165%, respectively. It is also stable towards detergents (5% DMSO and 1% Triton-X100), chelating reagent (1mM EDTA) and denaturing agent (1 M urea). The results show that CHIT42-SH16 from T. asperellum SH16 is able for further research such as a biocontrol for plant pathogens and hydrolysis of chitinous wastes

 Type: Domestic

 Author: Hoàng Tấn Quảng, Trần Thị Thu Hà, Trần Nguyên Thảo, Trần Thị Diễm Châu, Nguyễn Hoàng Lộc

 Unit: Laboratory of Gene technology

 Journal:Tạp chí Công nghệ Sinh học

 Issue, Number, Pages8, 3B, 1651-1657

 ISSN/ISBN:1859 - 2201

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 Year of publication: 2010

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