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KMID : 1007519940030010043
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Food Science and Biotechnology
1994 Volume.3 No. 1 p.43 ~ p.46
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Kinetic Properties of Aminopeptidase from Laetobaeillas casei AHU 1055
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Jung, Heon Woong
Jang, Hae Dong/Lee, Hyong Joo
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Abstract
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To investigate the kinetic properties of aminopeptidase purified from Lactobacillus casei AHU 1065, the effect of metal ions and chemicals on enzymatic activity, and substrate specificities of aminopeptidase were studied. The kinetic constants for 4 substrates (Leu-β-NA, Ala-β-NA, Pro-β-NA, Phe-β-NA) were estimated. The Km values of the towards these substrates were almost the same (1.7mM), However the Vmax values were quite different. The aminopeptidase was inhibited by the metal chelators, EDTA and 1,10-phenanthroline, but was reactivated with Co^(2+) and Mn^(2+). The aminopeptidase had a broad substrate specificity and hydrolyzed only substrates with hydrophobic amino acid at NH_(2)-terminal.
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KEYWORD
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