Purification and some properties of a chitinase from Xanthomonas sp. strain AK |
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Authors: | Yamaoka H Hayashi H Karita S Kimura T Sakka K Ohmiya K |
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Affiliation: | Faculty of Bioresources, Mie University, 1515 Kamihama-cho, Tsu 514-8507, Japan. |
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Abstract: | Chitinase B (ChiB) was purified from the culture supernatant of Xanthomonas sp. strain AK by Phenyl-Toyopearl 650M and DEAE-Toyopearl 650M column chromatographies. The purified enzyme preparation gave a single band on SDS-polyacrylamide gel electrophoresis and the molecular weight of ChiB was estimated to be 48,000. The enzyme was optimally active at pH 6.0 and 60 degrees C. N-Terminal amino acid sequence analysis suggested that ChiB is a member of glycosyl hydrolase family 18 and that it is genetically different from ChiA recently reported (Sakka et al., J. Ferment. Bioeng., 86, 527-533, 1998). Immunological analysis suggested that ChiB was the major chitinase species in the culture supernatant of Xanthomonas sp. strain AK and that production of the enzyme was induced by the presence of chitin. |
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