Isolation and Purification of Polypeptides from Morchella sextelata and Their Antioxidant Activity
Through alkaline extraction and acid precipitation,crude protein extract of Morchella sextelata fruiting bodies was obtained,and the extraction rate and protein content were 32.94％and 78.3％,respectively.Using degree of hydrolysis and DPPH scavenging rate of the resultant crude polypeptide as the indices,alkaline protease was then selected to digest the protein extract to yield crude polypeptide.The crude polypeptide was stepwise subjected to ultrafiltration DEAE-52 cellulose chromatography,and Sephadex G-25 gel filtration chromatography,and the resultant components of each step with high DPPH scavenging rate were used for the next purification.Eventually,two components SE-1 and SE-2 were obtained,and SE-1 had higher protein content and scavenging rates for DPPH,ABTS and·OH,reaching(86.7±1.75)％,(95.3±1.21)％and(80.6±1.35)％,respectively.The amino acid sequence of SE-1 was Gly-Gly-Pro-Pro-Gly-Gly-Glu-Asp-Gly-Gly-Gly-Phe-Gly-Gly-Met,and its relative molecular mass was 1 206.Under in vitro simulated gastrointestinal digestion conditions,the DPPH scavenging rate of SE-1 was high at 25-55 ℃,pH4-8 within 2 h digestion.
Morel sporocarp polypeptideisolation and purificationmass spectrometry identificationantioxidant activity
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维普
