A new, broad-substrate-specificity aminopeptidase from the dairy organism Lactobacillus helveticus SBT 2171

Article Abstract:

An aminopeptidase with a very broad substrate specificity was purified to homogeneity from Lactobacillus helveticus SBT 2171. It has a molecular mass of 95 kDa and an isoelectric point of 4.9. The enzyme hydrolyzed a large number of naphthylamide- and nitroanilide-substituted amino acids and several di-, tri- and oligopeptides. Experiments showed that the aminopeptidases from Lactococcus lactis and Lb. helveticus are immunologically different from each other.

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Degradation and debittering of a tryptic digest from beta-casein by aminopeptidase N from Lactococcus lactis subsp. cremoris Wg2

Article Abstract:

The effect of degradation of aminopeptidase N from Lactococcus lactis subsp. cremoris Wg2 on the bitter taste of a beta-casein tryptic digest was investigated. It was found that incubation of purified peptides with aminopeptidase N resulted in complete hydrolysis of many peptides. The degradation of the bitter tryptic digest by aminopeptidase N resulted in a decrease of hydrophobic peptides and in debittering of the peptide mixture.

Food and nutrition, Lactic acid, Casein

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Characterization of a prolidase from Lactobacillus delbrueckii subsp. bulgaricus CNRZ 397 with an unusual regulation of biosynthesis

Article Abstract:

A study was conducted to analyze the characterization of Lactobacillus delbrueckii subsp. bulgaricus CNRZ 397 by a high level of peptidase activities related to proline-supporting peptides. A prolidase was prepared to homogeneity and determined as a strict dipeptidase active on X-pro dipeptides. Results indicated that PepQ biosynthesis correlated with the composition of the culture medium.

Peptides, Biosynthesis

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