{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T00:11:54Z","timestamp":1788480714476,"version":"build-2803163510"},"reference-count":36,"publisher":"Wiley","issue":"14","license":[{"start":{"date-parts":[[2023,7,18]],"date-time":"2023-07-18T00:00:00Z","timestamp":1689638400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["U2006205"],"award-info":[{"award-number":["U2006205"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["32200021"],"award-info":[{"award-number":["32200021"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["scijournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["J Sci Food Agric"],"published-print":{"date-parts":[[2023,11]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:sec><jats:title>BACKGROUND<\/jats:title><jats:p>Marine 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.<\/jats:p><\/jats:sec><jats:sec><jats:title>RESULTS<\/jats:title><jats:p>The metalloprotease A69 from the marine bacterium <jats:italic>Anoxybacillus caldiproteolyticus<\/jats:italic> 1A02591 was successfully expressed in the food safe bacterium <jats:italic>Bacillus subtilis<\/jats:italic> as a secreted enzyme. A technique to efficiently produce protease A69 in a 15\u2010L bioreactor was established, with a production of 8988\u2009U\u2009mL<jats:sup>\u22121<\/jats:sup>. 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\u2009U\u2009g<jats:sup>\u22121<\/jats:sup> and 60\u2009\u00b0C for 3\u2009h. The prepared SPs had a high content (&gt;\u200990%) of peptides with a molecular mass less than 3000\u2009Da and contained 18 amino acids. The prepared SPs showed high angiotensin\u2010converting enzyme (ACE)\u2010inhibitory activity, with an IC<jats:sub>50<\/jats:sub> value of 0.135\u2009mg\u2009mL<jats:sup>\u22121<\/jats:sup>. Moreover, three ACE\u2010inhibitory peptides, RPSYT, VLIVP and LAIPVNKP, were identified from the SPs using liquid chromatography\u2010mass spectrometry analysis.<\/jats:p><\/jats:sec><jats:sec><jats:title>CONCLUSION<\/jats:title><jats:p>The 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. \u00a9 2023 Society of Chemical Industry.<\/jats:p><\/jats:sec>","DOI":"10.1002\/jsfa.12797","type":"journal-article","created":{"date-parts":[[2023,6,20]],"date-time":"2023-06-20T09:48:05Z","timestamp":1687254485000},"page":"7153-7163","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Production of marine bacterial metalloprotease <scp>A69<\/scp> and evaluation of its potential in preparing soybean peptides with angiotensin\u2010converting enzyme\u2010inhibitory 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