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This study aimed to isolate, clone, and express lipase-encoding genes from a potent bacterial source to produce a thermo-tolerant alkaline lipase with enhanced catalytic efficiency and practical applicability.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>\n                      Among several bacterial isolates, the most potent lipase producer was identified as\n                      <jats:italic>Lysinibacillus fusiformis<\/jats:italic>\n                      , and its 16\u00a0S rRNA sequence was deposited in GenBank (PP757498). Three lipase-encoding genes (\n                      <jats:italic>est<\/jats:italic>\n                      ,\n                      <jats:italic>est2<\/jats:italic>\n                      , and\n                      <jats:italic>lipA<\/jats:italic>\n                      ) were successfully isolated, cloned, and heterologously expressed in\n                      <jats:italic>Escherichia coli<\/jats:italic>\n                      BL21 (DE3). Their sequences were submitted to GenBank under accession numbers PX136937.1, PX136938.1, and PX136936.1, respectively. The recombinant lipase encoded by\n                      <jats:italic>lipA<\/jats:italic>\n                      (rLipase) exhibited the highest activity (150 U\/mL) compared with the native enzyme (56.2 U\/mL). Molecular docking analysis demonstrated strong binding affinity of rLipase toward major fatty acid derivatives in olive oil, with the highest affinity for linoleic acid (\u2212\u20098.0\u00a0kcal\/mol), followed by oleic acid (\u2212\u20097.8\u00a0kcal\/mol) and palmitic acid (\u2212\u20097.3\u00a0kcal\/mol). These interactions were stabilized by hydrophobic interactions and hydrogen bonding, with key contributions from critical amino acid residues, particularly VAL250. The partially purified recombinant lipase (rLipase) exhibited a maximum activity of 320 U\/mL at 80\u00a0\u00b0C and pH 9, demonstrating remarkable thermostability and alkaline tolerance. Functional evaluation showed that rLipase improved the detergent efficiency for oil stain-removal from cotton fabrics. In addition, supplementation with 0.4% rLipase accelerated Ras cheese ripening by shortening the maturation period from 120 to 90 days with maintaining the desired ripening process.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusions<\/jats:title>\n                    <jats:p>\n                      The recombinant lipase from\n                      <jats:italic>Lysinibacillus fusiformis<\/jats:italic>\n                      demonstrated high thermal stability, alkaline tolerance, and strong catalytic efficiency. Its effectiveness in detergent formulations and cheese ripening highlights its potential as a versatile industrial biocatalyst for lipid bioconversion and related applications.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1186\/s12934-026-03084-w","type":"journal-article","created":{"date-parts":[[2026,8,29]],"date-time":"2026-08-29T11:14:46Z","timestamp":1788002086000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Recombinant thermotolerant alkaline lipase from Lysinibacillus fusiformis for detergent and hard (Ras) cheese applications: cloning, expression, molecular docking, and characterization"],"prefix":"10.1186","volume":"25","author":[{"given":"Ghada M.","family":"El-Sayed","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3596-1250","authenticated-orcid":false,"given":"Hala R.","family":"Wehaidy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Adel M. 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