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Optimization of process conditions for production of angiotensin I-converting enzyme (ACE) inhibitory peptides from vital wheat gluten using response surface methodology

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Abstract

The degree of hydrolysis (DH) and angiotensin I-converting enzyme (ACE)-inhibitory activity of vital wheat gluten (VWG) hydrolyzed using Alcalase were investigated using Box-Behnken response surface methodology (RSM). The mean responses were fitted to a second order polynomial to obtain regression equations. The enzyme-substrate ratio and the hydrolysis time increased the DH significantly (p<0.05). The substrate concentration was the only significant linear term leading to an increase in ACE-inhibitory activity. The optimized conditions of a substrate concentration of 5.04%, an enzyme-substrate ratio 5.94%, and a hydrolysis time 30.79 min gave a point prediction of a 12.74% DH and 82.28% ACE-inhibitory activity. Analytical results from confirmatory experiment were a 12.22%±0.5 DH and a 78.93%±1.07 ACE-inhibitory activity. The optimized conditions of the study provide useful information to the functional food and beverage industries to enhance the anti-hypertensive activities of peptides from VWG.

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Correspondence to Haile Ma.

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Dadzie, R.G., Ma, H., Abano, E.E. et al. Optimization of process conditions for production of angiotensin I-converting enzyme (ACE) inhibitory peptides from vital wheat gluten using response surface methodology. Food Sci Biotechnol 22, 1531–1537 (2013). https://doi.org/10.1007/s10068-013-0248-9

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  • DOI: https://doi.org/10.1007/s10068-013-0248-9

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