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Position: Home > Articles > Separation, Purification and Activity of ACE Inhibitory Peptides from Oat FOOD SCIENCE 2010,31 (24) 222-229

燕麦ACE抑制肽的分离纯化及其活性研究

作  者:
王双;王昌涛;韩扬
单  位:
北京工商大学植物资源研究开发重点实验室
关键词:
燕麦;ACE抑制肽;大孔吸附树脂;凝胶层析
摘  要:
通过对3种大孔吸附树脂的比较,选择DA201-C树脂对燕麦ACE抑制肽进行纯化。纯化后的燕麦肽产物的ACE抑制率达到92.86%,利用HPLC测得纯化后燕麦ACE抑制肽的分子质量分布在240.10~1292.11D之间,这部分物质在整个纯化产物中占99.82%。采用SephadexG-15凝胶分离燕麦ACE抑制肽得到D峰,其IC50为0.103mg/mL,分子质量545D。采用大孔吸附树脂及凝胶层析法能够较好地分离纯化燕麦ACE抑制肽。
译  名:
Separation, Purification and Activity of ACE Inhibitory Peptides from Oat
作  者:
WANG Shuang1,2,WANG Chang-tao1,HAN Yang1 (1. Beijing Technology and Business University, Beijing Key Laboratory of Plant Resources Research and Development, Beijing 100048, China;2. College of Pharmaceutical, Heilongjiang University of Chinese Medicine, Harbin 150040, China)
关键词:
oat; ACE inhibitory peptide;macroporous resin; gel filtration chromatography
摘  要:
Through comparing three kinds of macroporous resins, DA201-C resin was selected to purify ACE inhibitory peptides from oat. The ACE inhibition rate of purified peptide from oat was 92.86%. The molecular mass of HPLC-purified oat ACE inhibitory peptides was the range of 240.10-1292.11 D. SephadexG-15 gel was used to purify ACE inhibitory peptides to obtain a fraction D with IC50 of 0.103 mg/ml and molecular weight of 545 D. Results indicated that macroporous resin and gel filtration chromatography could better purify ACE inhibitory peptides from oat.

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