Separation and Purification of ACE Inhibitory Peptides from Dual-Enzymatic Casein Hydrolysate

doi:10.7506/spkx1002-6630-201209011

Abstract

Abstract: ACE inhibitory peptides were prepared from casein by sequential hydrolysis with pepsin and trypsin. Casein hydrolysate was preliminarily separated with 6 ku MWCO ultrafiltration membrane and further purified by Sephadex G-15 column chromatography. The ACE inhibitory activity (IC50) of the separated fractions was determined by an in vitro assay, and their peptide profiles and molecular weights were measured by capillary electrophoresis (CE) and Q-TOF LC/MS, respectively. The results showed that IC50 values of casein hydrolysate, filtrate, and three fractions obtained by Sephadex G-15 column chromatography, factions Ⅰ, Ⅱ and Ⅲ were 560, 250, 123.41, 66.67μg/mL and 64.29μg/mL, respectively. FactionsⅠ, Ⅱ and Ⅲ were composed of 19, 14 and 5 peptides, respectively and their molecular weights ranged from 400 to 800 u.

Key words: casein, casein hydrolysate, ACE inhibitory peptide, pepsin, trypsin

CLC Number:

TS252.42

YANGMing，HUZhi-he. Separation and Purification of ACE Inhibitory Peptides from Dual-Enzymatic Casein Hydrolysate[J]. FOOD SCIENCE, 2012, 33(9): 50-53.

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Separation and Purification of ACE Inhibitory Peptides from Dual-Enzymatic Casein Hydrolysate

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