蛋清抗氧化肽分离纯化及结构鉴定

为了获得高活性、高纯度的蛋清抗氧化肽,以蛋清酶解物为原料,依次釆用超滤、离子交换色谱、凝胶色谱分离纯化抗氧化活性较强的肽段,运用基质辅助激光解吸离子化质谱解析肽链的氨基酸序列。结果表明:超滤法分离纯化EWPH所得的三个组分中,EWPH-Ⅲ(M_W<3 kDa)组分的DPPH自由基清除率最高,达到79.62%。离子交换层析分离纯化EWPH-III所得到的碱性组分B的DPPH自由基清除率最高,达到82.05%。凝胶过滤色谱分离EWPH-III-B所得到4组分中E组分的DPPH自由基清除率最高,为88.49%。高活性高纯度EWPH-III-B-E组分的相对分子质量为237.575,该二肽的氨基酸序列为丙氨酸-甲硫氨酸。

Isolation,Purification and Structural Identification of Aantioxidative Peptides from Egg White

In order to obtain high activity and high purity egg white antioxidant peptides, the egg white proteolytics were used as raw materials, and the peptides with strong antioxidant activity were separated and purified by ultrafiltration, ion exchange chromatography and gel chromatography. The amino acid sequence of the peptide chain was analyzed by matrix-assisted laser desorption ionization mass spectrometry. The results showed that the DPPH free radical scavenging rate of EWPH-III (MW<3 kDa) was up to 79.62% among the three components obtained by ultrafiltration separation and purification of EWPH. Among the two components obtained by ion exchange chromatography separation and purification of EWPH-III, the DPPH free radical scavenging rate of alkaline component B was up to 82.05%. The 4 components of EWPH-III-B were separated by gel filtration chromatography. The DPPH free radical scavenging rate of EWPH-III-B-E component was 88.49%. The relative molecular mass of EWPH-III-B-E was 237.575 and the amino acid sequence was Ala-Met.