Purification of chitinase/chitosanase from Bacillus cereus and discovery of an enzyme inhibitor

doi:10.1016/j.ijbiomac.2013.10.027

淡江大學機構典藏 > 理學院 > 化學學系暨研究所 > 期刊論文 > Item 987654321/93053

Please use this identifier to cite or link to this item: http://tkuir.lib.tku.edu.tw:8080/dspace/handle/987654321/93053

Title:	Purification of chitinase/chitosanase from Bacillus cereus and discovery of an enzyme inhibitor
Authors:	Liang, Tzu-Wen;Chen, Yue-Yin;Pan, Po-Shen;Wang, San-Lang
Contributors:	淡江大學化學學系
Keywords:	Bacillus cereus;Boron;Chitinase;Chitinase inhibitor;Chitosanase;Squid pen
Date:	2013-10-26
Issue Date:	2013-11-12 12:13:24 (UTC+8)
Publisher:	Amsterdam: Elsevier BV
Abstract:	A chitinase and a chitosanase were induced from a squid pen powder (SPP)-containing medium of Bacillus cereus TKU030 and purified by precipitation with ammonium sulphate and combined column chromatography. The purified chitinase and chitosanase exhibited optimum activity at 60 °C, pH 5–6 and 40 °C, pH 4, respectively. The chitinase and chitosanase were stable at 25–60 °C, pH 4–7 and 25–50 °C, pH 3–7, respectively. The chitinase and chitosanase showed the highest activity toward β-chitin and 60% DD chitosan, respectively. The chitinase was significantly inhibited by Mn2+ and EDTA but activated by Cu2+, Fe2+ and Ca2+. The chitosanase was significantly inhibited by Cu2+, Fe2+, Zn2+, Mn2+ and EDTA. The chitinase showed high stability in the presence of various surfactants, such as SDS, Tween 20, Tween 40 and Triton X-100. In contrast, these surfactants were inhibitors of the chitosanase. The chitinase and chitosanase were also inhibited by TKUPSP017, a small synthetic boron-containing molecule with a BF3K side-chain. However, TKUPSP017 enhanced the growth of B. cereus TKU030 in SPP-containing medium.
Relation:	International Journal of Biological Macromolecules 63, pp.8-14
DOI:	10.1016/j.ijbiomac.2013.10.027
Appears in Collections:	[化學學系暨研究所] 期刊論文

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