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Herein, we report a thermoresponsive hybrid nanomaterial (HM) composed of\n                    <jats:italic>Candida antarctica<\/jats:italic>\n                    fraction B (CALB) immobilized on gold nanoparticles (AuNPs) and coated with poly(\n                    <jats:italic>N<\/jats:italic>\n                    \u2010isopropylacrylamide) (PNIPAm). This system exhibits a reversible phase transition temperature (Tcp) at 33\u00b0C, enabling temperature\u2010dependent modulation of the enzymatic activity. Our data show that, below Tcp, the extended conformation of PNIPAm acts as a protective layer, limiting substrate access to the CALB catalytic site and inhibiting biocatalysis. Above Tcp, the collapsed PNIPAm chain exposes CALB to the medium, enabling the reaction to proceed with an approximately 5.6\u2010fold increase in the reaction rate. The HM displays reversible behavior in heating\u2010cooling cycles below and above Tcp, in contrast to free CALB, which follows a conventional temperature\u2010dependent response for enzymatic reactions. These findings demonstrate the use of thermoresponsive nanomaterials to enable indirect and reversible regulation of enzyme activity, providing an effective approach to tune biocatalysis across diverse reactions and enzyme systems.\n                  <\/jats:p>","DOI":"10.1002\/chem.71504","type":"journal-article","created":{"date-parts":[[2026,8,3]],"date-time":"2026-08-03T15:34:17Z","timestamp":1785771257000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Thermoresponsive Hybrid Nanostructures for Indirect Regulation of Lipase Activity"],"prefix":"10.1002","author":[{"given":"Ma\u00edra","family":"Theisen","sequence":"first","affiliation":[{"name":"Department of Chemistry Federal University of Paran\u00e1  Curitiba\u2010PR Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria C. 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