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Angiotensin- I Converting Enzyme Inhibitory Properties of Bovine Casein Hydrolysates in Different Enzymatic hydrolysis Conditions  

김현수 (축산기술연구소)
인영민 (축산기술연구소)
정석근 (축산기술연구소)
함준상 (축산기술연구소)
강국희 (성균관대학교 식품·생명자원학과)
이수원 (성균관대학교 식품·생명자원학과)
Publication Information
Food Science of Animal Resources / v.22, no.1, 2002 , pp. 87-93 More about this Journal
Abstract
Angiotensiri-I converting enzyme(ACE) catalyst the removal of the C-terminal dipeptide from the angiotensin-I to give the angiotensin-II, a potent peptide that causes constriction of regulation of blood pressure. Recently, ACE inhibitor peptides have been isolated from enzymatic digests of food protein. The aim of this study was to identify bovine casein hydrolysates with ACE inhibitory properties in different enzymatic hydrolysis conditions. The casein were hydrolyzed neutrase, alcalase, protamax, flavourzyme, premed 192, sumizyme MP, sumizyme LP and pescalase alone and with an enzyme combination. Premed 192 produced ACE inhibitory peptides most efficiently. In order to ACE inhibitory peptide produced enzymatic hydrolysis condition were premed 192 added to casein ratio of 1:100(w/w), and incubated at 47$\^{C}$ for 12hrs. Casein hydrolysate gave 50% inhibition(IC$\_$50/ value) of ACE activity at concentration with 248ug/ml(general method) and 265ug/ml(pretreatment method) respectively.
Keywords
angiotensin-I converting enzyme; casein; hydrolysate;
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