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Effect of Sodium Caseinate Hydrolysates on Angiotensin-I Converting Enzyme Inhibition Activity
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 Title & Authors
Effect of Sodium Caseinate Hydrolysates on Angiotensin-I Converting Enzyme Inhibition Activity
Lee, Keon-Bong; Shin, Yong-Kook; Baick, Seung-Chun;
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This study was carried out to identify the ACE (Angiotensin converting enzyme) inhibitory activity of casein hydrolysates for development of anti-hypertensive hydrolysates. Sodium caseinate was treated with six kinds of commercial proteases such as Flavourzyme, Protamex, Neutrase 1.5, Alcalase, Protease M, and Protease S for 8 h individually, and was then treated with the enzyme combination for 4 h at . The hydrolysate which had the highest ACE inhibitory effect was then hydrolysed successively with three digestive enzymes: pepsin, trypsin, and -chymotrypsin, at for 4 h under conditions mimicking those of the gastrointestinal tract. UF (ultra filtration) treatment was applied to one of the secondary hydrolysates to determine ACE inhibitory activity. When sodium caseinate was hydrolysed by commercial proteases, the degree of hydrolysis (DH) showed 2.54 to 4.25% and after secondary hydrolysis, DH showed 4.30 to 5.22%. ACE inhibitory activity and values decreased, and inhibition rates increased during hydrolysis. Protamex treatment showed the lowest value () and Flavourzyme hydrolysate showed the highest value (). As the first hydrolysate was treated with Flavourzyme, the ACE inhibitory activity increased. Neutrase hydrolysate had the highest activity with an value (). When Neutrase plus Flavourzyme treatment was hydrolyzed by digestive enzymes, the value () was decreased statistically (p<0.05). As Neutrase plus Flavourzyme hydrolysate is treated by UF with MW cut-off 10,000, permeate showed of value, showed no difference, but retentate which has over MW 10,000 showed statistically different value, (p<0.05).
angiotensin converting enzyme;sodium caseinate;hydrolysate;protease;digestive enzyme;
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돈피젤라틴 효소분해물의 항산화 활성 및 신경세포보호효과,김동욱;박기문;하고은;정주리;장운기;함준상;정석근;박범영;송진;장애라;

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