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Production and Characterization of a New alpha-Cyclodextrin Glycosyltransferase from a Marine Strain of Bacillus sp Y112

文献类型： 外文期刊

作者： Chen, Xiao-Tong; Huang, Li-Ping; Sun, Jing-Jing 1 ; Liu, Jun-Zhong 1 ; Wang, Wei 1 ; Sun, Mi 1 ; Hao, Jian-Hua 1 ;

作者机构： 1.Chinese Acad Fishery Sci, Key Lab Polar Fisheries Dev, Yellow Sea Fisheries Res Inst, Qingdao 266071, Peoples R China

2.Qingdao Natl Lab Marine Sci & Technol, Lab Marine Drugs & Bioprod, Qingdao 266071, Peoples R China

3.Qingdao Natl Lab Marine Sci &

关键词： alpha-Cyclodextrin Glycosyltransferase;Purification;Enzymatic Activity

期刊名称：JOURNAL OF BIOBASED MATERIALS AND BIOENERGY （ 影响因子：0.708； 五年影响因子：0.739 ）

ISSN： 1556-6560

年卷期： 2017 年 11 卷 3 期

页码：

收录情况： SCI

摘要： Cyclodextrin glycosyltransferase (CGTase) is an enzyme able to convert starch and other substrates into cyclodextrins (CDs). An alpha-cyclodextrin glycosyltransferase (alpha-CGTase) from the Bacillus sp. Y112, isolated from the Yellow Sea in China has been purified by ethanol precipitation, gel filtration and anion-exchange chromatography with a yield of 57.5%. The purified enzyme was a monomer and its molecular weight was estimated to be 90 kDa. The enzyme was stable over a pH range of 7.0 to 9.0 at 25 degrees C, with a maximum activity at pH 8.5. The purified alpha-CGTase was stable at 50 degrees C for at least 1 h, and the optimal temperature of the enzyme was 55 degrees C. The enzymatic activity increased in the presence of MnCl2 and MgCl2 but was strongly inhibited by AgCl. The maximum starch conversion in CDs was obtained after 6 h of cyclodextrin reaction, with the 66% of the total CDs content constituted by alpha-CD. Our findings indicated that Bacillus sp. Y112 is a novel source for CGTase production, useful for industrial starch processing and alpha-CD production.

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