Angiotensin‐converting enzyme (ACE) inhibitory peptides from fermented sausages inoculated with Lactobacillus plantarum CD101 and Staphylococcus simulans NJ201

Abstract

AbstractNatural ACE inhibitory peptides derived from food are considered to be an effective supplement for lowering blood pressure. This study investigated the effects of Lactobacillus plantarum CD101 and Staphylococcus simulans NJ201 on proteolysis and the sequence composition of ACE inhibitory peptides in fermented sausages. The ACE inhibitory activity of the inoculated group reached the maximum values on day 35 during the production of fermented sausages. A more positive effect in the hydrolysis of the sarcoplasmic and myofibrillar protein was observed in the inoculated group through sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS‐PAGE). The free amino acid content of the inoculated group was 865.21 ± 12.55 mg/100 g, which was significantly higher (P < 0.05) than that of the control group. The molecular weight distribution showed a significant increase (P < 0.05) in peptides with a molecular weight less than 1 kDa in the inoculated group. A total of thirty‐four peptides with high hydrophobicity were identified by liquid chromatograph‐mass spectrometer/mass spectrometer (LC–MS/MS). Furthermore, the peptides were isolated and purified using gel filtration chromatography (GFC) and reversed‐phased high‐performance liquid chromatography (RP‐HPLC). Eleven novel peptides were identified by Nano‐LC‐ESI‐MS/MS, in which VALSLSRP with X‐Pro structure exhibited the highest ACE inhibition rate (75.36 ± 2.45%). These results indicated that mixed starters are conducive to protein degradation and the formation of peptides with high ACE inhibitory activity, especially peptides less than 1 kDa, and could be used as a functional material for antihypertensive drugs.