Si trova su / Altri legami
© 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.
