Søren D. Nielsen

TL;DR: During processing and digestion, milk proteins are disassembled into peptides with an array of biological functions, including antimicrobial, angiotensin-converting enzyme inhibition, antioxidant, opioid, and immunomodulation, which are summarized in numerous reviews.

TL;DR: Overall, the stability of human milk Igs during gastric digestion is higher in preterm infant than in term infants, which could be beneficial for assisting the preterm infants’ immature immune system.

TL;DR: The number of peptides with high homology to known functional peptides increased from milk to the premature infant stomach and was greater from bovine milk proteins than human milk proteins, suggesting differential release of bioactive peptides from human and bovines milk proteins may impact overall health outcomes in premature infants.

TL;DR: Down-regulated expression of hilA and ssrB genes in S. Typhimurium DT104 wild-type strain was observed in the presence of La-5 and LH-2 CFSM, suggesting the importance of peptide transport by S. Typhoon for down regulation of virulence genes in Salmonella.

TL;DR: Whether proteolytic degradation of human milk proteins into peptides begins within the mammary gland is determined and which milk proteases participate in the proteolysis and which released peptides have bioactivity are predicted to be predicted.