Identification of novel peptides with high stability against in vitro hydrolysis from bovine elastin hydrolysates and evaluation of their elastase inhibitory activity

Abstract

Surviving in the gastrointestinal tract is crucial for biopeptides to exert physiological effects in vivo. To enrich elastase inhibitory peptides with high digestive stability, elastin peptides was separated by using ultrafiltration and macroporous resin column, then changes in elastase inhibitory activity, amino acid composition and peptide profile of elastin peptides during in vitro digestion were measured. The results revealed that the fraction F3 eluted by 40% ethanol displayed high digestive stability possibly due to the high content of Pro-containing peptides (20.25%). Particularly, thirty peptides in F3 exhibited high digestive stability and most of them contained GV and/or PG fragment. Since GV and PG could inhibit 35.70% and 51.77% elastase activity at the concentration of 20 mm, respectively, peptides in F3 survived in in vitro digestion which contained GV and PG sequence might be potential elastase inhibitors. This provides an approach for preparation of peptides with high bioactivity and digestive stability.