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KMID : 1007519970060040250
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Food Science and Biotechnology
1997 Volume.6 No. 4 p.250 ~ p.255
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Partial Purification and Characterization of Intracellular Aminopeptidase , Esterase , and Proteinase from Lactobacillus casei CC-12
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Park, Seung Yong
Shin, Joog Yup/Lee, Byong Hoon
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Abstract
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Intracellular aminopeptidase, esterase, proteinase of Lactobacillus casei CC-12 selected from various strains of Lactobacillus sp. were detected by API ZYM system. These enzymes were partially purified by a Fast Protein Liquid Chromatograph (FPLC) system consisted of an ion-exchange and a gel-filtration chromatography. Intracellular aminopeptidase, esterase and proteinase could be separated from the crude enzyme extracts by ion-exchange chromatography. The active fractions corresponding to each substrates were further purified by passing through gel-filtration column. The optimal pH for the activities of aminopeptidase and esterase were pH 7.2, and that of proteinase was pH 6.8. The optimal temperature of all the enzymes was 40℃. The intracellular enzymes were activated by Co^(2+), but aminopeptidase and proteinase were strongly suppressed by Cu^(2+). The activity of esterase was also stimulated by Ca^(2+) and Mg^(2+), and proteinase by Mn^(2+). Ethylenediaminetetraacetic acid(EDTA) inactivated aminopeptidase completely and inhibited proteinase strongly whereas phenylmethylsulphonylfluoride(PMSF) inhibited esterase strongly.
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