The occurrence of two intracellular oligoendopeptidases in Lactococcus lactis and their significance for peptide conversion in cheese

Applied Microbiology and Biotechnology
R BaankreisF A Exterkate

Abstract

Two intracellular oligopeptide-preferring endopeptidases have been detected in Lactococcus lactis. A neutral thermolysin-like oligoendopeptidase (NOP) has been purified to homogeneity and an alkaline oligoendopeptidase has been partially purified. The specificity of the oligoendopeptidases towards important intermediary cheese peptides, produced by chymosin action on the caseins, clearly differs from that of the cell-envelope proteinase (CEP). NOP is active under conditions prevailing in cheese and contributes to initial proteolysis in a young cheese. It probably plays a crucial role in the degradation of an important bitter peptide in cheese, the beta-casein 193-209 fragment. The relatively low activity of the alkaline endopeptidase is further suppressed in cheese by the highly competitive actions of NOP and CEP.

Citations

Oct 11, 2003·Biotechnology Advances·B C Saha, K Hayashi
Mar 4, 2014·Annual Review of Food Science and Technology·E J Smid, M Kleerebezem
Jun 4, 2011·International Journal of Food Microbiology·Irene BustosM Carmen Martínez-Cuesta
Nov 6, 2002·Journal of Dairy Science·T R TulerT R Klaenhammer
Jan 5, 2002·Applied and Environmental Microbiology·Camilla ChristenssonJulian R Reid
Oct 23, 2020·Food Science and Biotechnology·Peng SongZheng-Xiang Wang
Apr 1, 1997·Journal of Bacteriology·K M FensterJ L Steele

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