Characterization of halophilic alkaline phosphatase from Halomonas sp. 593, a moderately halophilic bacterium.
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.
Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University, Korimoto, Japan.
Matsujiro
M
Ishibashi
Sayaka
S
Yamashita
Masao
M
Tokunaga
D000469:Alkaline Phosphatase / Q000737:chemistry* / Q000378:metabolism*; D000595:Amino Acid Sequence; D004795:Enzyme Stability; D020632:Halomonas / Q000201:enzymology*; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D012965:Sodium Chloride / Q000737:chemistry
D012965:Sodium Chloride; D000469:Alkaline Phosphatase