干燥奈瑟菌SB中参与醋酸纤维素降解的酯酶碳水化合物结合模块的功能分析。

Functional analysis of the carbohydrate-binding module of an esterase from Neisseria sicca SB involved in the degradation of cellulose acetate.

作者信息

Moriyoshi Kunihiko, Koma Daisuke, Yamanaka Hayato, Ohmoto Takashi, Sakai Kiyofumi

机构信息

Environmental Technology Research Division, Osaka Municipal Technical Research Institute, Osaka, Japan.

出版信息

Biosci Biotechnol Biochem. 2010;74(9):1940-2. doi: 10.1271/bbb.100213. Epub 2010 Sep 7.

DOI:10.1271/bbb.100213

PMID:20834142

Abstract

An esterase gene from Neisseria sicca SB encoding CaeA, which catalyzes the deacetylation of cellulose acetate, was cloned. CaeA contained a putative catalytic domain of carbohydrate esterase family 1 and a carbohydrate-binding module (CBM) family 2. We constructed two derivatives, with and without the CBM of CaeA. Binding assay indicated that the CBM of CaeA had an affinity for cellulose.

摘要

克隆了来自干燥奈瑟菌SB的一个编码CaeA的酯酶基因，CaeA可催化醋酸纤维素的脱乙酰化反应。CaeA包含一个假定的碳水化合物酯酶家族1催化结构域和一个碳水化合物结合模块（CBM）家族2。我们构建了两个衍生物，一个带有CaeA的CBM，另一个没有。结合试验表明CaeA的CBM对纤维素具有亲和力。