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KMID : 0613820110210050761
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Journal of Life Science
2011 Volume.21 No. 5 p.761 ~ p.765
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Effect of NaCl on Hydrolytic Activity of Leucine Aminopeptidase from Bacillus sp. N2
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Chung Dong-min
Lee Gang-Deok
Chun Sung-sick
Chung Young-Chul
Chun Hyo-Kon
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Abstract
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Salt stability of enzymes is a crucial practical factor in the food industry. Previously, leucine aminopeptidase (LAP) was purified from Bacillus sp. N2. Here, we present the salt effect of LAP using synthetic substrates. LAP had a hydrolytic activity for L-leucine-ρ-nitroanilide in high concentrations of NaCl (up to 4 M), but not for other neutral salts (LiBr, LiCl, NaBr, KBr, and KCl). It hydrolyzed various synthetic di-peptide substrates with hydrophobic and hydrophilic amino acids at the C-terminal Xaa region, in the presence of 0-4 M NaCl. The result indicated that the hydrolytic action of LAP is not dependent on the hydrophobicity of the amino acid side chain at the scissile bond of the substrate. Remarkably, the hydrolytic activity of LAP was 1-3 folds higher than those of other LAPs and aminopeptidases in 4.5 M NaCl, suggesting that NaCl-tolerant LAP might be used in the food industry as cheese and anchovy sauce.
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KEYWORD
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Amino acid, Bacillus sp., exopeptidase, leucine aminopeptidase, salt
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