{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,21]],"date-time":"2026-10-21T13:40:25Z","timestamp":1792590025420,"version":"4.5.0"},"reference-count":0,"publisher":"The Scientific and Technological Research Council of Turkey (TUBITAK-ULAKBIM) - DIGITAL COMMONS JOURNALS","issue":"4","license":[{"start":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T00:00:00Z","timestamp":1787011200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Turkish Journal of Chemistry"],"abstract":"<jats:p>This study involved the immobilization of acetylcholinesterase (AChE) onto a natural thin membrane extracted from the inner epidermal layer of Allium cepa, with the aim of enhancing the enzyme\u2019s stability, activity, and reusability for potential biotechnological\u00a0applications. The membrane, composed of biocompatible polymers and naturally occurring functional groups, was used as a sustainable support in a combined strategy involving adsorption followed by glutaraldehyde-mediated cross-linking. Immobilization conditions\u00a0were optimized by evaluating key factors such as enzyme concentration, membrane quantity, cross-linker dosage, and contact time to achieve maximal catalytic efficiency. Structural and morphological changes on the membrane surface were assessed via scanning electron microscopy and infrared spectroscopy, confirming successful enzyme binding and alterations indicative of interaction. The\u00a0immobilized enzyme exhibited enhanced tolerance to pH and temperature variations when compared to its free form. While both free\u00a0and immobilized enzymes showed peak activity at 30 \u00b0C, the immobilized enzyme retained approximately 80% of its activity at 40 \u00b0C,\u00a0whereas the free enzyme retained only around 50%. A reusability assessment demonstrated that the immobilized system preserved over 60% of its initial activity after 10 consecutive cycles. Moreover, storage stability tests revealed that the immobilized enzyme maintained\u00a0nearly 40% of its catalytic function after 30 days at room temperature. These results highlight the effectiveness of the onion membrane\u00a0as a green and low-cost platform for enzyme immobilization, offering considerable promise for applications in industrial biocatalysis,\u00a0biosensing, and diagnostic technologies.<\/jats:p>","DOI":"10.55730\/1300-0527.3904","type":"journal-article","created":{"date-parts":[[2026,8,21]],"date-time":"2026-08-21T00:44:23Z","timestamp":1787273063000},"page":"386-400","source":"Crossref","is-referenced-by-count":0,"title":["Acetylcholinesterase immobilization on a natural thin membrane for stable\u00a0biocatalyst design"],"prefix":"10.55730","volume":"50","author":[{"ORCID":"https:\/\/orcid.org\/0009-0000-1588-6172","authenticated-orcid":true,"given":"S\u0130NEM","family":"\u00d6ZT\u00dcRK","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6883-0180","authenticated-orcid":true,"given":"CEYHUN","family":"I\u015eIK","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0000-0460","authenticated-orcid":true,"given":"MUSTAFA","family":"TEKE","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"34691","published-online":{"date-parts":[[2026,8,18]]},"container-title":["Turkish Journal of Chemistry"],"original-title":[],"language":"en","deposited":{"date-parts":[[2026,10,21]],"date-time":"2026-10-21T12:52:47Z","timestamp":1792587167000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.tubitak.gov.tr\/chem\/vol50\/iss4\/4"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8,18]]},"references-count":0,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2026,8,18]]}},"URL":"https:\/\/doi.org\/10.55730\/1300-0527.3904","relation":{},"ISSN":["1300-0527"],"issn-type":[{"value":"1300-0527","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,8,18]]}}}