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 Microbioljournal_title
Applied and environmental microbiologyauthors
Tan PS,van Kessel TA,van de Veerdonk FL,Zuurendonk PF,Bruins AP,Konings WNdoi
10.1128/AEM.59.5.1430-1436.1993subject
Has Abstractpub_date
1993-05-01 00:00:00pages
1430-6issue
5eissn
0099-2240issn
1098-5336journal_volume
59pub_type
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