Characterization of halophilic alkaline phosphatase from Halomonas sp. 593, a moderately halophilic bacterium |
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| Authors: | Ishibashi Matsujiro Yamashita Sayaka Tokunaga Masao |
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| Affiliation: | Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University, Korimoto, Japan. |
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| Abstract: | A halophilic alkaline phosphatase was highly purified (about 510-fold with about 21% yield) from a moderate halophile, Halomonas sp. 593. The N-terminal 35 amino acid sequence of this enzyme was found to be more acidic than those previously isolated from Vibrio spp., and this enzyme was partially resistant to SDS. Several enzymatic properties demonstrated that it showed higher halophilicity than those enzymes from Vibrio spp. |
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