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Comp Biochem Physiol B Biochem Mol Biol. 2010 Sep;157(1):26-32. doi: 10.1016/j.cbpb.2010.04.014. Epub 2010 May 9.

A novel cold-adapted cellulase complex from Eisenia foetida: characterization of a multienzyme complex with carboxymethylcellulase, beta-glucosidase, beta-1,3 glucanase, and beta-xylosidase.

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1
Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Sakai, Osaka, 599-8531, Japan. mueda@biochem.osakafu-u.ac.jp

Abstract

Clostridium sp. and some bacterial cellulases exist as an enzyme complex with cellulolytic, and hemicellulolytic enzymes, so called "cellulosome". In this article, we report that EF-CMCase25 occurs as a complex with beta-glucosidase, beta-1,3 glucanase, and beta-xylosidase. The multienzyme complex had a molecular mass of 150 kDa on gel filtration under non-reducing condition. After the gel filtration, the enzyme complex was purified to homogeneous state on BN-PAGE. The SDS-PAGE demonstrated that the purified protein is a complex with at least one CMCase (25 kDa), one beta-glucosidase (32 kDa), and one beta-1,3 glucanase (40 kDa) components. The CMCase activity in the purified enzyme complex at 15 degrees C was 44% of that obtained at the optimal temperature. The optimum pH of the EF-CMCase25 in the purified enzyme complex was pH 5.0 and stable at pH 7.0-9.0.

PMID:
20438857
DOI:
10.1016/j.cbpb.2010.04.014
[Indexed for MEDLINE]
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