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• W1990484651 abstract "Abstract A proteinase from Lactococcus lactis ssp. lactis IAM 1198 was purified to homogeneity by conventional Chromatographic techniques. The molecular mass of the enzyme was estimated to be 51 kDa by SDS-PAGE. Activity was maximal at pH 6.4 and 35 °C. The enzyme was stable at pH values from 6.0 to 8.0 and below 40 °C. The enzyme seemed to be a cysteine proteinase because it was inhibited by p -chloromercuriphenyl sulfonic acid. The Michaelis constant of the enzyme for carbobenzoxy- l -phenylalanyl- l -arginine-7-amido-4-methylcoumarin and l -arginine-7-amido-4-methylcoumarin was 6.9 M and 16.6 M, respectively. The enzyme showed both endopeptidase and aminopeptidase activity." @default.
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• W1990484651 date "1997-06-01" @default.
• W1990484651 modified "2023-09-27" @default.
• W1990484651 title "Purification and characterization of a cysteine proteinase from Lactococcus lactis ssp. lactis IAM 1198" @default.
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• W1990484651 doi "https://doi.org/10.1016/s0958-6946(97)00031-9" @default.
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