Enzyme Characterization of a New Strain of Chitinase
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    Abstract:

    Chitinase from a new isolated strain Chitinolyticbacter meiyuanensis SYBC-H1 was purified and characterized in this study.Chitinase of more than 95% purity was obtained after ammonium sulfate precipitation,DEAE-32 negative chromatography and Sephadex G-100 sieve chromatography.The results of enzyme properties indicated that its optimal pH and temperature was 40℃ and 6.5,respectively.Chitinase exposed to temperature lower than 50℃ was stable and it is most stable at pH 5.0.Its stability was promoted with the addition of mercaptoethanol and EDTA.Moreover,the chitinase activity was apparently stimulated by Na+ and K+,while inhibited by Zn2+,Mn2+,Fe2+ and Fe3+.The shrimp crust was hydrolyzed into acetylglucosamine by Chitinase from SYBC-H1,and the hydrolysis rate achieved at 21.8%.

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HAO Zhi-kui, CAI Yu-jie, LIAO Xiang-ru, HU Ming-ming, ZHANG Hai-rong, LI Jiao-yang, XING Yu-peng. Enzyme Characterization of a New Strain of Chitinase[J]. Journal of Food Science and Biotechnology,2011,30(5):705-710.

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  • Online: June 17,2014
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