Separation and purification of ACE inhibitory peptides from casein
Dai Yong-gang, Nan XiPing, Tiezhu Li, Zhennai Yang
Abstract
Dai Yong-gang, Nan XiPing, Tiezhu Li, Zhennai Yang
Abstract
ACE inhibitory peptides prepared by alkaline protease enzyme on casein were studied in this article.Optimized by orthogonal test,the optimum enzymatic hydrolysis conditions were:temperature 50 ℃,pH value 7.5,enzyme dosage 5%,substrate concentration 5%,under this conditions,the ACE inhibitory activity was 47.23%.Use of ultrafiltration on hydrolyzate for initial separation,obtained the molecular weight of less than 4 ku components,its ACE inhibitory activity was 57.34%.With gel filtration SephadexG-25 for further purification,the purified components of ACE inhibitory activity up to 62.78%,24.77% higher than the original hydrolysates,and its relative molecular weight was 1 500 u below.
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ACE inhibitory peptides prepared by alkaline protease enzyme on casein were studied in this article.Optimized by orthogonal test,the optimum enzymatic hydrolysis conditions were:temperature 50 ℃,pH value 7.5,enzyme dosage 5%,substrate concentration 5%,under this conditions,the ACE inhibitory activity was 47.23%.Use of ultrafiltration on hydrolyzate for initial separation,obtained the molecular weight of less than 4 ku components,its ACE inhibitory activity was 57.34%.With gel filtration SephadexG-25 for further purification,the purified components of ACE inhibitory activity up to 62.78%,24.77% higher than the original hydrolysates,and its relative molecular weight was 1 500 u below.
Key concepts: Chemistry, Chromatography, Ultrafiltration (renal), Casein, Hydrolysate, Protease, Enzyme, Size-exclusion chromatography