Separation and Purification of Anti-hypertensive Peptides from Pig Femoral Collagen

doi:10.7506/spkx1002-6630-2014060010

FOOD SCIENCE ›› 2014, Vol. 35 ›› Issue (6): 50-54.doi: 10.7506/spkx1002-6630-2014060010

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Separation and Purification of Anti-hypertensive Peptides from Pig Femoral Collagen

LIU Xiao-hong, LI Cheng*, FU Gang, SU Zhao

College of Food, Sichuan Agricultural University, Ya’an 625014, China

Received:2013-04-09 Revised:2014-03-08 Online:2014-03-25 Published:2014-04-04
Contact: LI Cheng E-mail:252903387@qq.com

Abstract

Abstract:

Anti-hypertensive peptides were prepared from pig femoral bones by sequential hydrolysis using alkaline
protease, papain and flavourzyme. In order to obtain high activity and purity of anti-hypertensive peptides, ultrafiltration, ion
exchange chromatography and gel permeation chromatography were used to separate the hydrolysates. The angioensin-Ⅰ
converting enzyme (ACE) inhibitory activity (IC50) of the separated fractions was determined in vitro. The results showed
that the ultrafiltration fraction with molecular weight of less than 5 ku showed the highest ACE inhibitory activity, with an
IC50 value of 1.400 2 mg/mL. The fraction was then purified by ion exchange chromatography to obtain 4 peaks, among
which peak 2 had the strongest ACE inhibitory activity with an IC50 value of 0.488 4 mg/mL. The peak 2 was further
fractionated by gel permeation chromatography to obtain 4 sub-peaks, and the sub-peak 2-2 had the highest ACE-inhibitory
activity with an IC50 value of 0.195 3 mg/mL.

Key words: enzymatic hydrolysis, anti-hypertensive peptides, ultrafiltration, ion exchange chromatography, gel permeation chromatography, half inhibitory concentration of angioensin-Ⅰ converting enzyme

CLC Number:

S879.9

LIU Xiao-hong, LI Cheng*, FU Gang, SU Zhao. Separation and Purification of Anti-hypertensive Peptides from Pig Femoral Collagen[J]. FOOD SCIENCE, 2014, 35(6): 50-54.

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Separation and Purification of Anti-hypertensive Peptides from Pig Femoral Collagen

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