Separation, Purification and Activity of ACE Inhibitory Peptides from Oat

doi:10.7506/spkx1002-6630-201024048

FOOD SCIENCE ›› 2010, Vol. 31 ›› Issue (24): 222-229.doi: 10.7506/spkx1002-6630-201024048

• Processing Technology • Previous Articles Next Articles

Separation, Purification and Activity of ACE Inhibitory Peptides from Oat

WANG Shuang1,2，WANG Chang-tao1,*，HAN Yang1

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

Received:2010-08-30 Online:2010-12-25 Published:2010-12-29
Contact: WANG Chang-tao1 E-mail:wangct@th.btbu.edu

Abstract

Abstract:

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.

Key words: oat, ACE inhibitory peptide, macroporous resin, gel filtration chromatography

CLC Number:

TS201.1

WANG Shuang1,2，WANG Chang-tao1,*，HAN Yang1. Separation, Purification and Activity of ACE Inhibitory Peptides from Oat[J]. FOOD SCIENCE, 2010, 31(24): 222-229.

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Separation, Purification and Activity of ACE Inhibitory Peptides from Oat

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