Production of angiotensin I-converting enzyme inhibitor derived from egg white protein hydrolysates using a membrane reactor

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Title:	Production of angiotensin I-converting enzyme inhibitor derived from egg white protein hydrolysates using a membrane reactor
Authors:	Chiang, W.-D., Tsou, M.-J., Weng, C.-H., Tsai, T.-C.
Contributors:	Department of Food Science, Tunghai University
Keywords:	chymotrypsin;dipeptidyl carboxypeptidase;egg protein;egg white;protein hydrolysate;proteinase;subtilisin;thermolysin
Date:	2008
Issue Date:	2013-06-19T09:02:49Z (UTC)
Abstract:	Egg white proteins (EWP) were hydrolyzed with four proteolytic enzymes, including Thermolysin, Alcalase, Esperase and Chymotrysin, to produce hydrolysates with angiotensin I-converting enzyme (ACE) inhibitory activity. The result indicated that EWP hydrolyzed for 0.5-24 hr with Thermolysin produced the highest ACE inhibitory activity among the four enzymes. Therefore, EWP-Thermolysin hydrolysate was produced and further fractionated using several membranes with molecular weight cut-off (MWCO) of 10,000, 3,000 and 1,000 daltons, sequentially. The 1 kDa permeate obtained from the hydrolysate treatment using 1,000 daltons MWCO membrane could further reduce its IC50 value from 54.1 to 17.2 μg protein/mL. A lower IC50 value represented higher ACE inhibitory activity. The operation stability study showed that the membrane reactor system could maintain a steady production of EWP-Thermolysin hydrolysate over 8 hr. The gastrointestinal protease in vitro effect on the ACE inhibitory activity of 1 kDa permeate indicated that gastrointestinal proteases have no significant effect (p > 0.05) on the ACE inhibitory activity of 1 kDa permeate.
Relation:	Journal of Food and Drug Analysis 16 (2) , pp. 54-60
Appears in Collections:	[食品科學系所] 期刊論文

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