The effect of starter cultures on peptide profiles identified in camel milk cheese

Cheese contains a lot of biologically active compounds; among them, peptides with functional properties are important assembles. In this study, camel milk cheese samples are studied. The camel milk was fermented by mesophilic and thermophilic cultures. Cheese samples were ripened for 30 days, and the peptides released from casein were analyzed using liquid chromatography–tandem mass spectrometry. Identified peptides were analyzed by applying chemometrics. Furthermore, peptides from camel milk cheeses (β-CN- and α-CN-derived) were identified using the milk bioactive peptides database (MBPDB) and Peptide Ranker. A total of 52 peptides were identified. In all, 21 peptides were identified from β-CN in cheeses using mesophilic culture and five peptides from α-CN besides 17 peptides from β-CN and nine peptides from α-CN in cheeses using thermophilic culture. From a biological point of view, the peptides identified in camel milk cheese were homologous to sequences that were previously reported in the literature to exhibit angiotensin-converting enzyme inhibitory, antioxidant, antimicrobial,and dipeptidyl-peptidase IV inhibitory activities based on peptide sequence databases.