阿胶酶解物抗氧化肽的分离与质谱分析

Isolation and mass spectrometric analysis of antioxidant peptides from enzymatic hydrolysates of roasted pills of Asini Corii Colla

采用阴离子交换纤维及Sephadex G-25柱色谱法对阿胶酶解物进行分离纯化,以DPPH,ABTS法对阿胶酶解物及其不同部位进行体外抗氧化能力测定,从阿胶酶解物中筛选出体外抗氧化活性最强的部位,命名为GFC-1。GFC-1质量浓度为2.0g·L-1时对DPPH清除率为47.95%,0.40g·L-1时对ABTS清除率为97.20%;利用LC-ESI-MS/MS结合TurboSE-QUEST检索软件及Swiss-Prot数据库从GFC-1中鉴定出9个小分子肽,并从中识别出高重复核心序列GPAGPP*GPP*(P*为羟脯氨酸)。

A fraction named GFC-1 with high antioxidant activities in vitro was isolated from the enzymatic hydrolysates of roasted pills of Asini Corii Calla, and the peptides in this fraction were identified. The enzymatic hydrolysates were isolated and purified with anion exchange chromatography and Sephadex G-25 filtration chromatography successively. GFC-1, a fraction isolated from the hydrolysates, exhibited the highest DPPH and ABTS scavenging capacity （DPPH 47.95% at 2. 0 g · L-1 and ABTS 97. 20% at O. 40 g · L-1 ）. Nine peptides from GFC-1 were identified by LC-ESI-MS/MS coupled with TurboSEQUEST search software and Swiss- Prot data base, and a high repetition core sequence GPAGPP ＊ GPP ＊ was also found.