Céline Cakir-Kiefer

TL;DR: This review focuses on different strategies that could be employed to enhance the production of bioactive peptides from the milk proteins that will be consequently used to functionalize the fermented milk products.

TL;DR: The degradation of proteins was characterised by electrophoresis and reversed-phase ultra-high performance liquid chromatography as discussed by the authors, and camel colostrum, colostral whey and milk proteins had unveiled angiotensin I-converting enzyme (ACE) inhibitory activity following in vitro enzymatic digestion and a higher free radical scavenging activity than before their digestion.

TL;DR: Investigation of peptide sequences homologous to known bioactive peptides highlighted not less than 16 different putative biological activities and the susceptibility of GlyCAM-1 towards bacterial proteolysis directly in milk was shown.

TL;DR: The stability of milk-derived bioactive peptides in this kind of products implies to carefully characterize the potential action of the surface proteolytic enzymes of S. thermophilus, especially when β-casomorphin-7 was used as substrate.

TL;DR: Results suggested the presence of cell-associated extracellular peptidase activities in S. thermophilus strains that could be vital for the growth of PrtS(-) strains.