Effect of NaCl on hydrolytic activity of leucine aminopeptidase from Bacillus sp. N2 = Bacillus sp. N2 유래 leucine aminopeptidase의 가수분해활성에 대한 NaCl의 영향

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Title
Effect of NaCl on hydrolytic activity of leucine aminopeptidase from Bacillus sp. N2 = Bacillus sp. N2 유래 leucine aminopeptidase의 가수분해활성에 대한 NaCl의 영향
Author(s)
Dong Min Chung; G D Lee; S S Chun; Y C Chung; Hyo Kon Chun
Bibliographic Citation
Korean Journal of Life Sciences, vol. 21, no. 5, pp. 761-765
Publication Year
2011
Abstract
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.
Keyword
Amino acidBacillus sp.exopeptidaseleucine aminopeptidasesalt
ISSN
I000-0052
Publisher
Korea Soc-Assoc-Inst
DOI
http://dx.doi.org/10.5352/JLS.2011.21.5.761
Type
Article
Appears in Collections:
Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
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