2010Zhongguo rupin gongyeRequires access

Separation and purification of ACE inhibitory peptides from casein

Dai Yong-gang, Nan XiPing, Tiezhu Li, Zhennai Yang

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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.

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Available 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.

Key concepts: Chemistry, Chromatography, Ultrafiltration (renal), Casein, Hydrolysate, Protease, Enzyme, Size-exclusion chromatography

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