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Journal of Dairy Science Vol. 75 No. 1 27-35
© 1992 by American Dairy Science Association ®
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Purification and Characterization of an Aminopeptidase from Lactobacillus helveticus LHE-511

Hiroshi Miyakawa 1, Susumu Kobayashi 1, Seiichi Shimamura 1, and Mamoru Tomita 1

1 Nutritional Science Laboratory, Morinaga Milk Industry Co., Ltd., 1-83, 5-Chome, Higashihara, Zama-City, Kanagawa-Pref., Japan 228

A cell-surface bound aminopeptidase from Lactobacillus helveticus LHE-511 was purified and characterized. The enzyme was found to have a monomeric structure and a molecular mass of 92 kDa. The optimal pH and temperature for activity were 7.0 and 37°C respectively. The enzyme was strongly activated by Co2+, completely inhibited by chelating reagents such as EDTA and 1,10-phenanthroline, and weakly inhibited by p-chloromercuribenzoate, suggesting that it is a metalloenzyme possessing a thiol group at its activity site. The enzyme showed high activity with p-nitroaniline derivatives or dipeptides and tripeptides that have a hydrophobic amino acid (Leu, AIa, or Phe) or diaminomonocarboxylic acid (Lys or Arg) at the N terminus.

Key Words: Lactobacillus helveticus • aminopeptidase • cheese • ripening

Submitted on November 7, 1990
Accepted on July 25, 1991




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Appl. Envir. Microbiol., July 1, 1999; 65(7): 3001 - 3007.
[Abstract] [Full Text]


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