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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