Affiliation:
1. FB Biologie/Chemie, Universität Osnabrück, 49069 Osnabrück, Germany,1 and
2. National Institute of Agro-Environmental Sciences, Tsukuba, Ibaraki 305-8604, Japan2
Abstract
ABSTRACT
Upstream of the
Streptomyces coelicolor
A3(2) chitinase G gene, a small gene (named
chb3
) is located whose deduced product shares 37% identical amino acids with the previously described CHB1 protein from
Streptomyces olivaceoviridis
. The
chb3
gene and its upstream region were cloned in a multicopy vector and transformed into the plasmid-free
Streptomyces lividans
TK21 strain. The CHB3 protein (14.9 kDa) was secreted by the
S. lividans
TK21 transformant during growth in the presence of glucose,
N
-acetylglucosamine, yeast extract, and chitin. The protein was purified to homogeneity using anionic exchange, hydrophobic interaction chromatographies, and gel filtration. In contrast to CHB1, CHB3 targets α-chitin, β-chitin, and chitosan at pH 6.0 but does so relatively loosely. The ecological implications of the divergence of substrate specificity of various types of chitin-binding proteins are described.
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
Cited by
23 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献