{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,29]],"date-time":"2026-10-29T20:17:47Z","timestamp":1793305067299,"version":"4.5.0"},"reference-count":53,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2024,1,23]],"date-time":"2024-01-23T00:00:00Z","timestamp":1705968000000},"content-version":"vor","delay-in-days":22,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"content-domain":{"domain":["enviromicro-journals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Microbial Biotechnology"],"published-print":{"date-parts":[[2024,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    In the current trend where plant\u2010based foods are preferred over animal\u2010based foods, pulses represent an alternative source of protein but also of bioactive peptides (BPs). We investigated the pattern of protein hydrolysis during fermentation of red lentils protein isolate (RLPI) with various lactic acid bacteria and yeast strains.\n                    <jats:italic>Hanseniaspora uvarum<\/jats:italic>\n                    SY1 and\n                    <jats:italic>Fructilactobacillus sanfranciscensis<\/jats:italic>\n                    E10 were the most proteolytic microorganisms.\n                    <jats:italic>H. uvarum<\/jats:italic>\n                    SY1 led to the highest antiradical, angiotensin\u2010converting enzyme\u2010inhibitory and antifungal activities, as found in low molecular weight water soluble extracts (LMW\u2010WSE). The 2039 peptide sequences identified by LMW\u2010WSE were screened using BIOPEP UWM database, and 36 sequences matched with known BPs. Fermentation of RLPI by lactic acid bacteria and yeasts generated 12 peptides undetected in raw RLPI. Besides,\n                    <jats:italic>H. uvarum<\/jats:italic>\n                    SY1 led to the highest abundance (peak areas) of BPs, in particular with antioxidant and ACE\u2010inhibitory activities. The amino acid sequences LVR and LVL, identified in the fermented RLPI, represent novel findings, as they were detected for the first time in substrates subjected to microbial fermentation. KVI, another BP highly characteristic of RLPI\u2010SY1, was previously observed only in dried bonito. 44 novel potential BPs, worthy of further characterization, were correlated with antifungal activity.\n                  <\/jats:p>","DOI":"10.1111\/1751-7915.14387","type":"journal-article","created":{"date-parts":[[2024,1,24]],"date-time":"2024-01-24T02:50:06Z","timestamp":1706064606000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":27,"title":["Lentils protein isolate as a fermenting substrate for the production of bioactive peptides by lactic acid bacteria and neglected yeast species"],"prefix":"10.1111","volume":"17","author":[{"given":"Stefano","family":"Tonini","sequence":"first","affiliation":[{"name":"Faculty of Agricultural, Environmental and Food Sciences Free University of Bolzano\u2010Bozen  Bolzano 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