{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T03:49:27Z","timestamp":1790394567846,"version":"4.1.0"},"reference-count":60,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2025,9,26]],"date-time":"2025-09-26T00:00:00Z","timestamp":1758844800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003827","name":"National Research, Development and Innovation Office","doi-asserted-by":"publisher","award":["FK 134886"],"award-info":[{"award-number":["FK 134886"]}],"id":[{"id":"10.13039\/501100003827","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003827","name":"National Research, Development and Innovation Office","doi-asserted-by":"publisher","award":["TKP2021-EGA-28"],"award-info":[{"award-number":["TKP2021-EGA-28"]}],"id":[{"id":"10.13039\/501100003827","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100020916","name":"Hungarian Research Network","doi-asserted-by":"crossref","award":["HUN-REN 2001007"],"award-info":[{"award-number":["HUN-REN 2001007"]}],"id":[{"id":"10.13039\/100020916","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["www.mdpi.com"],"crossmark-restriction":true},"short-container-title":["Biomolecules"],"abstract":"<jats:p>Commercial fungal lipases from Rhizopus oryzae, Rhizopus niveus, Aspergillus niger, Rhizomucor miehei, and Candida rugosa were immobilized via physical adsorption onto Accurel MP 1000, a hydrophobic polypropylene support. The effects of enzyme concentration, pH, temperature, and glutaraldehyde post-treatment were systematically evaluated. Immobilization generally enhanced enzyme stability, which was further improved in several cases by glutaraldehyde crosslinking. The immobilized preparations retained over 50% of their initial activity for 3\u20136 cycles, and 7\u201310 cycles following glutaraldehyde treatment. While soluble enzymes lost nearly all activity within three months at 5 \u00b0C and 25 \u00b0C and retained only 5\u201320% at \u221220 \u00b0C, the immobilized forms preserved 50\u2013100% of their activity under all storage conditions tested. Immobilized lipases also exhibited improved thermal stability at 60 \u00b0C by general increments between 1.3 and 1.8 times compared to soluble lipases. Increased tolerance to pH fluctuations was observed in most immobilized enzymes, particularly from R. oryzae, R. niveus, R. miehei, and C. rugosa. Organic solvent tolerance of the immobilized enzymes showed highest stability in hexane (66\u2013100% residual activity after 4 h incubation). Glutaraldehyde treatment affected solvent stability of immobilized lipases in enzyme and solvent dependent manner. These findings demonstrate the improved stability and applicability of the produced biocatalysts in varying reaction environments.<\/jats:p>","DOI":"10.3390\/biom15101372","type":"journal-article","created":{"date-parts":[[2025,9,26]],"date-time":"2025-09-26T15:25:59Z","timestamp":1758900359000},"page":"1372","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Enhancing the Stability of Fungal Lipases by Immobilization onto Accurel MP 1000 Support and Additional Glutaraldehyde Crosslinking"],"prefix":"10.3390","volume":"15","author":[{"given":"Alexandra","family":"Kov\u00e1cs-Kotog\u00e1n","sequence":"first","affiliation":[{"name":"Department of Biotechnology and Microbiology, Faculty of Science and Informatics, University of Szeged, K\u00f6z\u00e9p fasor 52, H-6726 Szeged, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8211-5431","authenticated-orcid":false,"given":"Tam\u00e1s","family":"Papp","sequence":"additional","affiliation":[{"name":"Department of Biotechnology and Microbiology, Faculty of Science and Informatics, University of Szeged, K\u00f6z\u00e9p fasor 52, H-6726 Szeged, Hungary"},{"name":"HUN-REN-SZTE Pathomechanisms of Fungal Infections Research Group, University of Szeged, K\u00f6z\u00e9p fasor 52, H-6726 Szeged, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0009-7773","authenticated-orcid":false,"given":"Csaba","family":"V\u00e1gv\u00f6lgyi","sequence":"additional","affiliation":[{"name":"Department of Biotechnology and Microbiology, Faculty of Science and Informatics, University of Szeged, K\u00f6z\u00e9p fasor 52, H-6726 Szeged, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1219-1049","authenticated-orcid":false,"given":"Mikl\u00f3s","family":"Tak\u00f3","sequence":"additional","affiliation":[{"name":"Department of Biotechnology and Microbiology, Faculty of Science and Informatics, University of Szeged, K\u00f6z\u00e9p fasor 52, H-6726 Szeged, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,9,26]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"6223","DOI":"10.1039\/C3CS60075K","article-title":"Enzyme immobilisation in biocatalysis: Why, what and how","volume":"42","author":"Sheldon","year":"2013","journal-title":"Chem. 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