{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T17:04:07Z","timestamp":1790010247292,"version":"4.0.1"},"reference-count":47,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T00:00:00Z","timestamp":1789948800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Science and Technology Development Project of Jilin Province","award":["20250601055RC"],"award-info":[{"award-number":["20250601055RC"]}]}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Nutr."],"abstract":"<jats:p>\n                    Carboxypeptidases, a class of exopeptidases that specifically cleave C-terminal amino acid residues from peptide chains, are extensively utilized for food component modification and quality enhancement. This review focuses on the three-dimensional structural characteristics and active-site catalytic mechanisms of serine carboxypeptidases, metallocarboxypeptidases, and cysteine carboxypeptidases and describes the construction and optimization strategies for heterologous expression systems, with particular emphasis on\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    (\n                    <jats:italic>E. coli<\/jats:italic>\n                    ),\n                    <jats:italic>Bacillus subtilis<\/jats:italic>\n                    , and\n                    <jats:italic>Pichia pastoris<\/jats:italic>\n                    . Furthermore, the use and current research status of carboxypeptidases in food processing are comprehensively explored, including the debittering of protein hydrolysates, the targeted preparation of high-Fischer-ratio (high-F-ratio) oligopeptides, the quality enhancement of fermented foods, and the green biological detoxification of ochratoxin A (OTA). Further research can focus on enhancing the substrate specificity and catalytic efficiency of carboxypeptidases through molecular modification. This review aims to provide a theoretical foundation for the broader application of carboxypeptidases in green food manufacturing and quality improvement.\n                  <\/jats:p>","DOI":"10.3389\/fnut.2026.1915795","type":"journal-article","created":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T16:14:46Z","timestamp":1790007286000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":0,"title":["Carboxypeptidases for food processing: structural characteristics, expression optimization, and advances in applications"],"prefix":"10.3389","volume":"13","author":[{"given":"Yitong","family":"Du","sequence":"first","affiliation":[{"name":"College of Food Science and Engineering, Jilin Agricultural University","place":["Changchun, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Junqi","family":"Liu","sequence":"additional","affiliation":[{"name":"College of Food Science and Engineering, Jilin Agricultural University","place":["Changchun, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xinyu","family":"Zhu","sequence":"additional","affiliation":[{"name":"College of Food Science and Engineering, Jilin Agricultural University","place":["Changchun, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ting","family":"Yu","sequence":"additional","affiliation":[{"name":"Department of Nutrition, The Second Hospital of Jilin University","place":["Changchun, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiyan","family":"Wang","sequence":"additional","affiliation":[{"name":"College of Food Science and Engineering, Jilin Agricultural University","place":["Changchun, 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