期刊
JOURNAL OF FUNCTIONAL FOODS
卷 65, 期 -, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.jff.2019.103751
关键词
Protease; Pseudomonas aeruginosa; Wheat gluten; Antihypertensive peptides
资金
- National Key Basic Research and Development Plan of China Modern Food Processing, Storage, and Transportation Technology and Equipment [2017YFD0400200]
The feasibility of a protease of Pseudomonas aeruginosa (PaproA) to prepare angiotensin I-converting enzyme (ACE) inhibitory peptides from wheat gluten was evaluated according to physiochemical and antihypertensive performances. The wheat gluten hydrolyzed by Alcalase plus PaproA (WGH_APae) to produce small fragments (<1 kDa) was particularly preferred by the superior protein recovery rate, degree of hydrolysis, ACE inhibitory potential, and stability against gastrointestinal digestion. Among the resultant fractions from WGH_APae, the lower IC50 value of fraction 7 indicated proper concentrations of proline and negatively charged amino acids were critical to modulate ionic and hydrophobic interactions on ACE catalytic sites to inhibit ACE activity. Subsequently, fraction 7 was purified to identify two successful antihypertensive peptides containing tryptophan at the carboxyl-end: SAGGYIW and APATPSFW with IC50 values of 0.002 mg/mL and 0.036 mg/mL, respectively, suggesting both peptides had potentials in the nutraceuticals and functional foods to prevent and/or treat hypertension.
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