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Preparation and Properties of Bioactive Peptides from Yeast Protein
並列摘要
The peptides were prepared from yeast protein using yeast hydrolytic enzyme. The bioactivity of yeast peptides after impurity removal (YP1) was detected in vitro. MWCO-5kDa ultrafiltration membrane was employed to separate the yeast protein hydrolysates. Equally, the bioactivity of yeast peptides after ultrafiltration (YP2) was detected in vitro. The results showed that after ultrafiltration, bioactive components were enriched. YP2 revealed stronger superoxide anion scavenging, α-glucosidase inhibitory and ACE inhibitory activities than YP1, with the IC50 value of 2.60mg/mL, 10.62mg/mL, and 29.32μg/mL, respectively. Results of molecular weight distribution measured by FPLC indicated that, the content of YP2lower than 1kDa was 80.41%, with MW1kDa-3kDa was about 18.36%, while the residues were with MW3kDa-5kDa. The study on chemical stability and biological stability illuminated that YP2 components showed good acid-base stability, thermal stability and resistance to digestion stability.
延伸閱讀
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