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The antihypertensive activity of yeast hydrolysate (YH) was confirmed in our previous study. However, the critical peptides in YH and the underlying mechanisms have not been fully elucidated. This study aimed to explore the angiotensin-converting enzyme (ACE) inhibitory peptides in YH and illustrate their molecular and cellular mechanisms. The potential of YH-derived peptides was evaluated by in silico methods, followed by in vitro verification. A new competitive ACE inhibitory peptide, VIPVPFF (V7), with an IC50 value of 10.27 μM, was screened. YH and V7 increased the nitric oxide (NO) levels, upregulated GUCY1A1 gene expression (approximately 15-fold), and functioned in several hypertension-related pathways in human umbilical vein endothelial cells (HUVECs). This study revealed the antihypertensive mechanisms of YH and V7, laying down a theoretical basis for their application.

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Butelase-1 is an efficient ligase from Clitoria ternatea with wide applications in the food and biopharmaceutical fields. This research aimed to achieve high-efficiency expression of butelase-1 and explore its application in food-derived angiotensin I-converting enzyme (ACE) inhibitory peptides. The recombinant butelase-1 zymogen was prepared at a yield of 100 mg/L in Escherichia coli and successfully activated at pH 4.5, resulting in a 6973.8 U/L yield of activated butelase-1 with a specific activity of 348.69 U/mg and a catalytic efficiency of 9956 M–1 s–1. Activated butelase-1 exhibited considerable resistance to Tween-20, Triton X-100, and methanol. The “traceless” cyclization of ACE inhibitory peptides was realized using activated butelase-1, which resulted in higher stability and ACE inhibitory activity than those of the linear peptides. Our work proposed an efficient method for the preparation of butelase-1 and provided a promising model for its application in food fields.