大豆肽的离子交换色谱分离及其活性评价

Isolation and identification of ACE inhibition peptides from soy hydrolytes with ionic-exchange chromatograph

采用Sephadex C-25阳离子交换剂对经过DA201-C型大孔吸附树脂脱盐、乙醇梯度洗脱(75%乙醇洗脱组分)的Alcalase水解大豆肽(DH14%)进行进一步的分离纯化,并对分离得到的各组分ACE抑制活性进行了评价。试管试验确定的SephadexC-25色谱分离条件为:上样量0.004g/mLIE,起始缓冲液为1M醋酸,上样吸附率为61.19%。经SP-Sephadex C-25分离得到6个组分,其中未吸附的3个组分ACE抑制活性低,但NaCl梯度洗脱的3个组分ACE活性均为60%左右,从纯化ACE抑制活性肽的角度考虑,分离效果比SephadexG-15差。

Sephadex C-25 was used for further fractionation of ACE inhibi- tion soy peptides obtained from Alcalase hydrolyzation （ DH14% ） and gradient ethanol elution with DA201-C maeroporous adsorption resin （ 75% ethanol fraction）. Fraetionation parameters with Sphadex C-25 were decided by test tube experiment, the optimal parameters were as follows： loading capacity 0. 004 g/mL IE, starting buffer 1M acetic acid, adsorption ratio 61.69%. Six fractions were obtained after NaCl gradient elution, among which 3 were unabsorbed fractions. ACE inhibition activity of the 3 NaCl eluted fractions were all about 60%, which means the fractionation effect of Sphadex C-25 was not as good as gel filtration chromatograph Sephadex G-15 in terms of ACE inhibition peptides.