Identification of lactoferrin peptides generated by digestion with human gastrointestinal enzymes

摘要: Lactoferrin (LF) is a protein present in milk and other body fluids that plays important biological roles. As part of diet, LF must survive gastrointestinal conditions or create bioactive fragments to exert its effects. The degradation formation peptides highly dependent on individual variation intraluminal composition. study was designed compare the peptide bovine (bLF) following vitro digestion under different simulated conditions. Human (GI) juices were used 2-step model mimic stomach duodenum. To account for buffering capacity lactoferrin-containing foods, gastric pH adjusted either slowly rapidly 2.5 4.0. results compared with vivo bLF performed 2 volunteers. High concentration GI fast reduction resulted complete step. More resisted when reduced Several identified; however, few matched previously reported from studies using nonhuman enzymes. Surprisingly, no lactoferricin, f(17–41), identified during used. diversity enzymes human seems affect hydrolysis bLF, generating those obtained only one proteases animal origin. Multiple sequence analysis indicated motif consisting proline neighboring hydrophobic residues could restrict proteolytic processing. Further structure showed almost all cutting sites located surface mainly nonglycosylated half lactoferrin. Digestion by may generate found lactoferrin digested tract should be taken into consideration health effects are proposed, because has now been approved European Food Safety Authority as dietary supplement food products.