摘要
采用DA201-C型大孔吸附树脂对Alcalase水解,DH14%的大豆肽进行脱盐和乙醇分布洗脱,不同浓度乙醇洗脱物的氨基酸组成分析结果表明:洗脱是按照疏水性递增的方式进行的。乙醇浓度为75%时洗脱下来的组分都具有最高的降血压活性,其ACE抑制率为56.52%。体外模拟实验测定结果表明:经过胃肠道酶的作用,大豆肽的ACE抑制活性仍达到49.52%。采用1M的醋酸作为洗脱液可以实现75%乙醇洗脱组分的SephadexG-15有效分离,其中ACE抑制活性最强组分的抑制率为69.57%,IC50为0.144mg/mL。
Macroporous adsorption resin DA201-C and Sephadex G-15 gel filtration chromatograph were used for fractionation of ACE inhibition peptides from Alcalase hydrolyzed soy protein （ DH14% ）. Amino acid analysis results suggested that soy peptides were eluted from DA201-C according to its hydrophobicity with gradient ethanol elution. ACE inhibition activity of 75% ethanol elution fraction was 56.52%, which was the highest among 4 soy peptide fractions. Vivo test showed that ACE inhibition activity of this fraction was still 49. 52% after pepsin and pencreatin treatment. Further fractionation of this fraction was performed on Sephadex G- 15 using 1 M acetic acid as elution buffer. As for the most active ACE inhibition fraction, the ACE inhibition activity was 69. 57%, IC50 0. 144 mg/mL.
出处
《食品与机械》
CSCD
北大核心
2006年第4期25-28,45,共5页
Food and Machinery
