Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Microbiology & Fermentation Technology Note
Characterization of Halophilic Alkaline Phosphatase from Halomonas sp. 593, a Moderately Halophilic Bacterium
Matsujiro ISHIBASHISayaka YAMASHITAMasao TOKUNAGA
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2005 年 69 巻 6 号 p. 1213-1216

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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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© 2005 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
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