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

Abstract:

:The mode of action of purified aminopeptidase N from Lactococcus lactis subsp. cremoris Wg2 on a complex peptide mixture of a tryptic digest from bovine beta-casein was analyzed. The oligopeptides produced in the tryptic digest before and after aminopeptidase N treatment were identified by analysis of the N- and C-terminal amino acid sequences and amino acid compositions of the isolated peptides and by on-line liquid chromatography-mass spectrometry. Incubation of purified peptides with aminopeptidase N resulted in complete hydrolysis of many peptides, while others were only partially hydrolyzed or not hydrolyzed. The tryptic digest of beta-casein exhibits a strong bitter taste, which corresponds to the strong hydrophobicity of several peptides in the tryptic digest of beta-casein. The degradation of the "bitter" tryptic digest by aminopeptidase N resulted in a decrease of hydrophobic peptides and a drastic decrease of bitterness of the reaction mixture.

journal_name

Appl Environ Microbiol

authors

Tan PS,van Kessel TA,van de Veerdonk FL,Zuurendonk PF,Bruins AP,Konings WN

doi

10.1128/AEM.59.5.1430-1436.1993

subject

Has Abstract

pub_date

1993-05-01 00:00:00

pages

1430-6

issue

5

eissn

0099-2240

issn

1098-5336

journal_volume

59

pub_type

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