Research on marine bioactive peptides has mainly focused on characterization of peptides in hydrolysates prepared with commercial industrial enzymes and the usefulness of such hydrolysates in health and functional foo...Research on marine bioactive peptides has mainly focused on characterization of peptides in hydrolysates prepared with commercial industrial enzymes and the usefulness of such hydrolysates in health and functional foods. However, a relevant question is whether digestion of fish proteins with gastrointestinal proteases per se generates peptides that also can have health promoting properties and can reduce, e.g., diabetes 2, inflammation and hypertension either in relation to gastrointestinal digestion or as alternative to industrial proteases. The aim of the study was to investigate hydrolysates obtained from in vitro sequential digestion of salmon muscle and skin with gastrointestinal proteases including pepsin, pancreatic and pancreatic ＋ mucosal proteases for their ability to scavenge ABTS^＋ radicals and inhibit activity of angiotensin I-converting enzyme （ACE） and dipeptidyl peptidase 4 （DPP-4）. Furthermore, it was the aim to study the inhibitory mechanism and stability towards ACE and DPP-4 activity. Analysis of〈 10 kDa hydrolysates showed that gastrointestinal proteases generated peptides with clear radical scavenging activity and DPP-4 and ACE inhibiting activity as well. Hydrolysates from pepsin digestion exhibited the lowest ECso values for radical scavenging activity and ACE inhibition, whereas ECso increased in hydrolysates after subsequent digestion with pancreatic and mucosal proteases. Interestingly, ECso values for the DPP-4 inhibition were hardly affected by sequential digestion. Inhibition modes for the muscle hydrolysates were both competitive and non-competitive, but prolonged incubation showed that the inhibitory properties were unstable and therefore they were probably digested as competitive substrates by gastrointestinal proteases.展开更多
文摘Research on marine bioactive peptides has mainly focused on characterization of peptides in hydrolysates prepared with commercial industrial enzymes and the usefulness of such hydrolysates in health and functional foods. However, a relevant question is whether digestion of fish proteins with gastrointestinal proteases per se generates peptides that also can have health promoting properties and can reduce, e.g., diabetes 2, inflammation and hypertension either in relation to gastrointestinal digestion or as alternative to industrial proteases. The aim of the study was to investigate hydrolysates obtained from in vitro sequential digestion of salmon muscle and skin with gastrointestinal proteases including pepsin, pancreatic and pancreatic ＋ mucosal proteases for their ability to scavenge ABTS^＋ radicals and inhibit activity of angiotensin I-converting enzyme （ACE） and dipeptidyl peptidase 4 （DPP-4）. Furthermore, it was the aim to study the inhibitory mechanism and stability towards ACE and DPP-4 activity. Analysis of〈 10 kDa hydrolysates showed that gastrointestinal proteases generated peptides with clear radical scavenging activity and DPP-4 and ACE inhibiting activity as well. Hydrolysates from pepsin digestion exhibited the lowest ECso values for radical scavenging activity and ACE inhibition, whereas ECso increased in hydrolysates after subsequent digestion with pancreatic and mucosal proteases. Interestingly, ECso values for the DPP-4 inhibition were hardly affected by sequential digestion. Inhibition modes for the muscle hydrolysates were both competitive and non-competitive, but prolonged incubation showed that the inhibitory properties were unstable and therefore they were probably digested as competitive substrates by gastrointestinal proteases.
