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 alpha-chitin, beta-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.
journal_name
Appl Environ Microbioljournal_title
Applied and environmental microbiologyauthors
Saito A,Miyashita K,Biukovic G,Schrempf Hdoi
10.1128/AEM.67.3.1268-1273.2001keywords:
subject
Has Abstractpub_date
2001-03-01 00:00:00pages
1268-73issue
3eissn
0099-2240issn
1098-5336journal_volume
67pub_type
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