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- W1978414063 startingPage "1164" @default.
- W1978414063 abstract "Some physical and chemical properties and substrate specificity were investigated of the neutral protease obtained from B. amylosacchariticus, a strain of saccharogenic a-amylase-producing Bacillus subtilis. The molecular weight and sedimentation coefficient of the pro-tease were estimated to be 33, 800 and 3.02, respectively, by ultracentrifugal analyses, and alanine was identified as an amino-terminal amino acid of the enzyme by the Sanger's method. The enzyme showed more broad specificity than the neutral protease of liquefying α-amylase-producing B. subtilis, when tested with synthetic peptides, and hippuryl-L-leucin-amide was the best substrate among 42 compounds tested. On a long incubation, the enzyme hydrolyzed several proteins in a degree of 10 to 25% as peptide bond cleavage." @default.
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- W1978414063 date "1966-01-01" @default.
- W1978414063 modified "2023-09-24" @default.
- W1978414063 title "Studies on Bacterial Protease" @default.
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- W1978414063 doi "https://doi.org/10.1271/bbb1961.30.1164" @default.
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