中国食品学报2011，Vol.11Issue(8)：16-22,7.
卵白蛋白抗氧化肽分离与纯化
Isolation and Purification of Antioxidant Peptide from Ovalbumin
摘要
Abstract
Objective:Isolation antioxidative peptide from ovalbumin by enzymatic hydrolysis. Method:Antioxidative peptides in the hydrolysates were purified by ultrafiltration (UF) membrane system, Q-Sepharose FF ion-exchang chro-matography and Teverse phase high-perfomiance liquid chromatography (RP-HPLC). Their structure was further identified by electrospray ionization tandem mass spectrometry (ESI-MS/MS). Result:Three peptides with strong antioxidative activities were purified from the hydrolysates. Their structure were Pro-Glu-Tyr (MWL:408.14Da), Leu-Pro-Asp-Glu(MW: 473.19 Da) and Trp-Val-Glu(MW: 433.18), which are 115-117th, 245-248th and 148-150th amino acid residuces in the sequence of ovalbumin, respectively. Conclusion:Three antioxidative peptides were obtained from hydrolysates of ovalbumin by pepsin.关键词
卵白蛋白/酶解/抗氧化肽/分离Key words
ovalbumin/enzymatic hydrolysis/antioxidative peptide/isolation引用本文复制引用
沈勇根,徐明生,尹忠平,吴少福..卵白蛋白抗氧化肽分离与纯化[J].中国食品学报,2011,11(8):16-22,7.基金项目
江西省教育厅项目(GJJ98134) （GJJ98134）
