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International Journal of Food Sciences and Nutrition Volume 67, 2016 - Issue 2
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In Vitro and Animal Studies

Digestion and absorption of an egg white ACE-inhibitory peptide in human intestinal Caco-2 cell monolayers

Long DingLaboratory of Nutrition and Functional Food, Jilin University, Changchun, P.R. China;
,
Liying WangLaboratory of Nutrition and Functional Food, Jilin University, Changchun, P.R. China;
,
Zhipeng YuCollege of Food Science and Engineering, Bohai University, Jinzhou, P.R. China
,
Ting ZhangLaboratory of Nutrition and Functional Food, Jilin University, Changchun, P.R. China;
&
Jingbo LiuLaboratory of Nutrition and Functional Food, Jilin University, Changchun, P.R. China; Correspondence[email protected]
Pages 111-116 | Received 15 Oct 2015, Accepted 13 Jan 2016, Published online: 16 Feb 2016
 
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Abstract

The objective of this study was to investigate the digestion and absorption of egg white-derived angiotensin I-converting enzyme (ACE)-inhibitory peptide TNGIIR in human intestinal Caco-2 cell monolayers. Results showed that the digestion of TNGIIR to simulated gastrointestinal enzymes and brush border membrane peptidases were 5.87% ± 1.92% and 17.17% ± 0.64%, respectively (p < 0.05). The apparent permeability coefficients (Papp) of TNGIIR from the apical to basolateral side in Caco-2 cell monolayers was determined to be (4.92 ± 0.40) × 10−6 cm/s, indicating that TNGIIR can transport across Caco-2 cell monolayers in intact form. In addition, only cytochalasin D, a disruptor of tight junctions (TJs), changed TNGIIR transport rate significantly (p < 0.05), suggesting that the main transport route for TNGIIR across Caco-2 cell monolayers was paracellular pathway via TJs.

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