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KMID : 1024620020220010087
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Food Science of Animal Resources
2002 Volume.22 No. 1 p.87 ~ p.93
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Angiotensin- I Converting Enzyme Inhibitory Properties of Bovine Casein Hydrolysates in Different Enzymatic hydrolysis Conditions
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Kim Hyun-Soo
In Young-Min
Ham Jun-Sang
Kang Kook-Hee
Lee Soo-Won
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Abstract
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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 for 12hrs. Casein hydrolysate gave 50% inhibition(IC50/ value) of ACE activity at concentration with 248ug/ml(general method) and 265ug/ml(pretreatment method) respectively.
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KEYWORD
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angiotensin-I converting enzyme, casein, hydrolysate
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