Preparation of ACE inhibitory peptides from Tenebrio molitor and antibacterial activity

Abstract

This research aimed to obtain active peptides that exert remarkable inhibitory effects on Angiotensin-converting enzyme (ACE). The ACE inhibitory peptides from T. molitor were were prepared by hydrolyzing Tenebrio molitor powders with papain, separated by using ultrafiltration membranes. Five molecular weight fractions were obtained. Sephadex G-15 was used to separate the fraction with molecular weight < 3 kDa through the different concentrations of the enzyme solutions. Results showed that 100 mg/mL was the optimal concentration, and the elution peaks were divided into three groupsM1,M2,M3. The M2 component showed the highest activity,which was analyzed and found to be abundant and diverse. The molecular weight of M2, which was composed of three amino acid residues. The inhibitory activities of the enzymatic hydrolysis solution, the ultrafiltration component, and the chromatography component against indicator bacteria were measured. The enzymatic hydrolysis solution and the component >30 kDa in molecular weight exhibited inhibitory effects on the three indicator bacteria.