碱性蛋白酶酶解鸡蛋清抗氧化肽的分离纯化

用碱性蛋白酶水解蛋清制备酶解液,通过超滤、离子交换、凝胶层析等手段对鸡蛋清酶解液抗氧化肽进行分离纯化并用薄层层析检验其纯度。研究表明,鸡蛋清酶解液经超滤除去杂蛋白,经DEAE-52离子层析分离出5个组分,其中组分2的抗氧化活性最强,超氧阴离子半抑制(IC50)质量浓度为13.32mg/mL,纯化倍数为2.51,蛋白回收率为25.04%。组分2经Sephadex G-25葡聚糖凝胶进一步分离得3个组分,其中组分3超氧阴离子的清除活性最强,其IC50为5.63mg/mL,纯化倍数达到5.93,蛋白回收率为13.42%,经薄层层析检测为单点,说明蛋清抗氧化肽得到纯化。

Purification of antioxidant peptides derived from egg white hydrolysised by alcalase

The egg white protein was hydrolyzed with alcalase and the antioxidant peptides were obtained through fractionating on ultrafiltration,ion-exchange chromatography and gel filtration chromatography.After the removal of hybrid proteins in hydrolysates,five fractions were obtained on DEAE-52 cellulose Ion-exchange column and fraction 2 showed the highest antioxidant activity with the IC50 values of superoxide anion radical scavenging 13.32 mg/mL.The purifrcation fold was 2.51 and recovery rate was 25.04%.Fraction 2 was further separated into 3 subfractions by Sephadex G-25,and subfraction 3 showed highest superoxide anion radical scavenging activities and the IC50 value was 5.63 mg/mL,purifrcation fold was 5.93,recovery rate was 13.42%.The thin-layer chromatography and dyeing results illustrated the antioxidant peptides had been purified.