Characteristics of a Streptomyces coelicolor A3(2) extracellular protein targeting chitin and chitosan

Autor(en): Saito, A
Miyashita, K
Biukovic, G
Schrempf, H 
Stichwörter: ALPHA-CHITIN; BINDING PROTEIN; Biotechnology & Applied Microbiology; CHB1; CLONING; DIRECT REPEAT SEQUENCES; EXPRESSION; GENE; Microbiology; NUCLEOTIDE-SEQUENCE; OLIVACEOVIRIDIS; PURIFICATION
Erscheinungsdatum: 2001
Herausgeber: AMER SOC MICROBIOLOGY
Journal: APPLIED AND ENVIRONMENTAL MICROBIOLOGY
Volumen: 67
Ausgabe: 3
Startseite: 1268
Seitenende: 1273
Zusammenfassung: 
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.
ISSN: 00992240
DOI: 10.1128/AEM.67.3.1268-1273.2001

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