{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T11:04:39Z","timestamp":1790247879851,"version":"4.1.0"},"reference-count":94,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T00:00:00Z","timestamp":1788480000000},"content-version":"vor","delay-in-days":3,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["ift.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Comp Rev Food Sci Food Safe"],"published-print":{"date-parts":[[2026,9]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Lipase activity in grains is a critical factor limiting the shelf\u2010life of whole\u2010grain flours and brans. Inside intact kernels, lipase and its substrates are separated by structural barriers. Once lipase is in contact with the substrate (triacylglycerols, TAGs) after milling, it hydrolyzes TAGs into free fatty acids (FFAs), and the grain matrices become rancid, a condition known as hydrolytic rancidity. Further oxidation of FFAs produces aldehydes and ketones, generating off\u2010flavors and compromising sensory quality and product acceptability. This review consolidates recent advances in lipase inactivation using various thermal, nonthermal, ozone exposure, and salt conditioning across different grain matrices. Superheated steam and atmospheric cold plasma were the most effective thermal and nonthermal treatments, respectively, achieving 100% and 97% lipase inactivation in wheat, while salt conditioning provided only partial activity (55%) suppression. The extent of inactivation depends on the matrices and grain type, treatment type, and intensity. Lipase inactivation kinetics were described using first, fractional, and\n                    <jats:italic>n<\/jats:italic>\n                    th\u2010order models, and the rate constants (\n                    <jats:italic>k<\/jats:italic>\n                    , min\n                    <jats:sup>\u22121<\/jats:sup>\n                    ) were compared across treatments and grain types. The effects of residual lipase activity and storage stability of lipids in grain\u2010based matrices were evaluated using mixed correlation and multivariate analyses. The unifying mechanistic outcome was disruption of the lipase lid domain and catalytic triad, and changes in conformational structures, though the reversibility of these structural changes varied across treatments. Thus, this review provides a cross\u2010grain comparative framework to guide the design of grain\u2010specific lipase stabilization strategies for producing shelf\u2010stable whole\u2010grain flour and bran products.\n                  <\/jats:p>","DOI":"10.1111\/1541-4337.70629","type":"journal-article","created":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T17:26:06Z","timestamp":1788542766000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Inactivation of Lipase in Grains: Processing Methods, Kinetics, and Storage Stability"],"prefix":"10.1111","volume":"25","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7586-8571","authenticated-orcid":false,"given":"Snehasis","family":"Chakraborty","sequence":"first","affiliation":[{"name":"Department of Grain and Food Science Kansas State University  Manhattan Kansas USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Suhan Bheemaiah","family":"Balyatanda","sequence":"additional","affiliation":[{"name":"Department of Grain and Food Science Kansas State University  Manhattan Kansas USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Harshavardhan Reddy","family":"Settipalli","sequence":"additional","affiliation":[{"name":"Department of Grain and Food Science Kansas State University  Manhattan Kansas USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bindusri","family":"Naraharasetti","sequence":"additional","affiliation":[{"name":"Department of Grain and Food Science Kansas State University  Manhattan Kansas USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4038-2790","authenticated-orcid":false,"given":"Kaliramesh","family":"Siliveru","sequence":"additional","affiliation":[{"name":"Department of Grain and Food Science Kansas State University  Manhattan Kansas USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,9,4]]},"reference":[{"key":"e_1_2_15_2_1","doi-asserted-by":"publisher","DOI":"10.3390\/molecules28052298"},{"key":"e_1_2_15_3_1","doi-asserted-by":"publisher","DOI":"10.1111\/1541\u20104337.12594"},{"key":"e_1_2_15_4_1","doi-asserted-by":"publisher","DOI":"10.3389\/fpls.2022.962667"},{"key":"e_1_2_15_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.biochi.2010.03.023"},{"key":"e_1_2_15_6_1","doi-asserted-by":"publisher","DOI":"10.1007\/s13562\u2010022\u201000787\u20100"},{"key":"e_1_2_15_7_1","doi-asserted-by":"publisher","DOI":"10.1007\/s00299\u2010021\u201002714\u20104"},{"key":"e_1_2_15_8_1","doi-asserted-by":"publisher","DOI":"10.1007\/s12298\u2010023\u201001343\u20103"},{"key":"e_1_2_15_9_1","doi-asserted-by":"publisher","DOI":"10.1590\/S0104\u201066322010000100002"},{"key":"e_1_2_15_10_1","first-page":"89","volume-title":"Lipases","author":"Br\u00eada G. 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