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.

根据理化和降压性能，评估了铜绿假单胞菌蛋白酶（PaproA）从小麦面筋中制备血管紧张素I转换酶（ACE）抑制肽的可行性。通过Alcalase加PaproA（WGH_APae）水解以产生小片段（<1 kDa）的小麦面筋，由于其优异的蛋白质回收率，水解度，ACE抑制潜能和对胃肠道消化的稳定性而特别受青睐。在WGH_APae的馏分中，较低的IC ₅₀馏分7的值表明脯氨酸和带负电荷的氨基酸的适当浓度对于调节ACE催化位点上的离子和疏水相互作用以抑制ACE活性至关重要。随后，将馏分7纯化，以鉴定两个成功的在羧基端含色氨酸的降压肽：SAGGYIW和APATPSFW，IC ₅₀值分别为0.002 mg / mL和0.036 mg / mL，表明这两种肽在营养保健品和功能性食品中均具有潜力。预防和/或治疗高血压的食物。