Production of marine bacterial metalloprotease A69 and evaluation of its potential in preparing soybean peptides with angiotensin‐converting enzyme‐inhibitory activity

Abstract

AbstractBACKGROUNDMarine bacteria secrete a variety of proteases, which are a good source to explore proteases with application value. However, only a few marine bacterial proteases with a potential in bioactive peptides preparation have been reported.RESULTSThe metalloprotease A69 from the marine bacterium Anoxybacillus caldiproteolyticus 1A02591 was successfully expressed in the food safe bacterium Bacillus subtilis as a secreted enzyme. A technique to efficiently produce protease A69 in a 15‐L bioreactor was established, with a production of 8988 U mL−1. Based on optimizing the hydrolysis parameters of A69 on soybean protein, a process for soybean protein peptides (SPs) preparation was set up, in which soybean protein was hydrolyzed by A69 at 4000 U g−1 and 60 °C for 3 h. The prepared SPs had a high content (> 90%) of peptides with a molecular mass less than 3000 Da and contained 18 amino acids. The prepared SPs showed high angiotensin‐converting enzyme (ACE)‐inhibitory activity, with an IC50 value of 0.135 mg mL−1. Moreover, three ACE‐inhibitory peptides, RPSYT, VLIVP and LAIPVNKP, were identified from the SPs using liquid chromatography‐mass spectrometry analysis.CONCLUSIONThe marine bacterial metalloprotease A69 has a promising potential for preparing SPs with good nutritional and potential antihypertensive effects, laying a good foundation for its industrial production and application. © 2023 Society of Chemical Industry.