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Release of angiotensin I converting enzyme (ACE) inhibitory activity during in vitro gastrointestinal digestion: from batch experiment to semicontinuous model

Vanessa Vermeirssen (UGent) , John Van Camp (UGent) , Liesbeth Devos (UGent) and Willy Verstraete (UGent)
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Abstract
Gastrointestinal digestion is of major importance in the bioavailability of angiotensin I converting enzyme (ACE) inhibitory peptides, bioactive peptides with possible anti hypertensive effects. In this study, the conditions of in vitro gastrointestinal digestion leading to the formation and degradation of ACE inhibitory peptides were investigated for pea and whey protein. In batch experiments, the digestion simulating the physiological conditions sufficed to achieve the highest ACE inhibitory activity, with IC50 values of 0.076 mg/mL for pea and 0.048 mg/mL for whey protein. The degree of proteolysis did not correlate with the ACE inhibitory activity and was always higher for pea than whey. In a semicontinuous model of gastrointestinal digestion, response surface methodology studied the influence of temperature and incubation time in both the stomach and small intestine phases on the ACE inhibitory activity and degree of proteolysis. For pea protein, a linear model for the degree of proteolysis and a quadratic model for the ACE inhibitory activity could be constituted. Within the model, a maximal degree of proteolysis was observed at the highest temperature and the longest incubation time in the small intestine phase, while maximal ACE inhibitory activity was obtained at the longest incubation times in the stomach and small intestine phase. These results show that ACE inhibitory activity of pea and whey hydrolysates can be controlled by the conditions of in vitro gastrointestinal digestion.
Keywords
ACE inhibitory peptides, pea protein, whey protein, response surface methodology, WHEY PROTEINS, ANTIHYPERTENSIVE PEPTIDES, BETA-LACTOGLOBULIN, HYPERTENSIVE RATS, BLOOD-PRESSURE, MILK-PROTEINS, FOOD PROTEINS, PROTEOLYSIS, INVITRO, HYDROLYSATE

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Chicago
Vermeirssen, Vanessa, John Van Camp, Liesbeth Devos, and Willy Verstraete. 2003. “Release of Angiotensin I Converting Enzyme (ACE) Inhibitory Activity During in Vitro Gastrointestinal Digestion: From Batch Experiment to Semicontinuous Model.” Journal of Agricultural and Food Chemistry 51 (19): 5680–5687.
APA
Vermeirssen, Vanessa, Van Camp, J., Devos, L., & Verstraete, W. (2003). Release of angiotensin I converting enzyme (ACE) inhibitory activity during in vitro gastrointestinal digestion: from batch experiment to semicontinuous model. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 51(19), 5680–5687.
Vancouver
1.
Vermeirssen V, Van Camp J, Devos L, Verstraete W. Release of angiotensin I converting enzyme (ACE) inhibitory activity during in vitro gastrointestinal digestion: from batch experiment to semicontinuous model. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY. 2003;51(19):5680–7.
MLA
Vermeirssen, Vanessa, John Van Camp, Liesbeth Devos, et al. “Release of Angiotensin I Converting Enzyme (ACE) Inhibitory Activity During in Vitro Gastrointestinal Digestion: From Batch Experiment to Semicontinuous Model.” JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 51.19 (2003): 5680–5687. Print.
@article{211201,
  abstract     = {Gastrointestinal digestion is of major importance in the bioavailability of angiotensin I converting enzyme (ACE) inhibitory peptides, bioactive peptides with possible anti hypertensive effects. In this study, the conditions of in vitro gastrointestinal digestion leading to the formation and degradation of ACE inhibitory peptides were investigated for pea and whey protein. In batch experiments, the digestion simulating the physiological conditions sufficed to achieve the highest ACE inhibitory activity, with IC50 values of 0.076 mg/mL for pea and 0.048 mg/mL for whey protein. The degree of proteolysis did not correlate with the ACE inhibitory activity and was always higher for pea than whey. In a semicontinuous model of gastrointestinal digestion, response surface methodology studied the influence of temperature and incubation time in both the stomach and small intestine phases on the ACE inhibitory activity and degree of proteolysis. For pea protein, a linear model for the degree of proteolysis and a quadratic model for the ACE inhibitory activity could be constituted. Within the model, a maximal degree of proteolysis was observed at the highest temperature and the longest incubation time in the small intestine phase, while maximal ACE inhibitory activity was obtained at the longest incubation times in the stomach and small intestine phase. These results show that ACE inhibitory activity of pea and whey hydrolysates can be controlled by the conditions of in vitro gastrointestinal digestion.},
  author       = {Vermeirssen, Vanessa and Van Camp, John and Devos, Liesbeth and Verstraete, Willy},
  issn         = {0021-8561},
  journal      = {JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY},
  keyword      = {ACE inhibitory peptides,pea protein,whey protein,response surface methodology,WHEY PROTEINS,ANTIHYPERTENSIVE PEPTIDES,BETA-LACTOGLOBULIN,HYPERTENSIVE RATS,BLOOD-PRESSURE,MILK-PROTEINS,FOOD PROTEINS,PROTEOLYSIS,INVITRO,HYDROLYSATE},
  language     = {eng},
  number       = {19},
  pages        = {5680--5687},
  title        = {Release of angiotensin I converting enzyme (ACE) inhibitory activity during in vitro gastrointestinal digestion: from batch experiment to semicontinuous model},
  url          = {http://dx.doi.org/10.1021/jf034097v},
  volume       = {51},
  year         = {2003},
}

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