{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T17:48:38Z","timestamp":1790358518205,"version":"4.1.0"},"reference-count":51,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2025,1,21]],"date-time":"2025-01-21T00:00:00Z","timestamp":1737417600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Multilateral Project Partenariats Hubert Curien (PHC)-Maghreb 2020 Program of the French Ministry of Foreign Affairs and Ministry of Higher Education and Research","award":["FranMaghZYM 2020-2024"],"award-info":[{"award-number":["FranMaghZYM 2020-2024"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>This work describes the immobilization and the characterization of purified Penicillium crustosum Thom P22 lipase (PCrL) using adsorption, encapsulation, and adsorption\u2013encapsulation approaches. The maximum activity of the immobilized PCrL on CaCO3 microspheres and sodium alginate beads was shifted from 37 to 45 \u00b0C, compared with that of the free enzyme. When sodium alginate was coupled with zeolite or chitosan, the immobilization yield reached 100% and the immobilized PCrL showed improved stability over a wide temperature range, retaining all of its initial activity after a one-hour incubation at 60 \u00b0C. The immobilization of PCrL significantly improves its catalytic performance in organic solvents, its pH tolerance value, and its thermal stability. Interestingly, 95% and almost 50% of PCrL\u2019s initial activity was retained after 6 and 12 cycles, respectively. The characteristics of all PCrL forms were analyzed by X-ray diffraction and scanning electron microscopy combined with energy dispersive spectroscopy. The maximum conversion efficiency of oleic acid and methanol to methyl esters (biodiesel), by PCrL immobilized on CaCO3, was 65% after a 12 h incubation at 40 \u00b0C, while free PCrL generated only 30% conversion, under the same conditions.<\/jats:p>","DOI":"10.3390\/molecules30030434","type":"journal-article","created":{"date-parts":[[2025,1,21]],"date-time":"2025-01-21T04:19:51Z","timestamp":1737433191000},"page":"434","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["Preparation and Biochemical Characterization of Penicillium crustosum Thom P22 Lipase Immobilization Using Adsorption, Encapsulation, and Adsorption\u2013Encapsulation Approaches"],"prefix":"10.3390","volume":"30","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2949-7463","authenticated-orcid":false,"given":"Ismail","family":"Hasnaoui","sequence":"first","affiliation":[{"name":"G\u00e9nie Enzymatique, Membranes Biomim\u00e9tiques et Assemblages Supramol\u00e9culaires (GEMBAS), Institut de Chimie et de Biochimie Mol\u00e9culaires et Supramol\u00e9culaires (ICBMS), UMR 5246 CNRS, Univ Lyon, Universit\u00e9 Lyon 1, B\u00e2t Raulin, 43 Bd du 11 Novembre 1918, F-69622 Villeurbanne cedex, France"},{"name":"Laboratoire de Bioressources, Biotechnologie, Ethnopharmacologie et Sant\u00e9 (LBBES), Facult\u00e9 des Sciences d\u2019Oujda (FSO), Universit\u00e9 Mohammed Premier (UMP), Bd Mohamed VI BP 717, Oujda 60000, Morocco"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sondes","family":"Mechri","sequence":"additional","affiliation":[{"name":"Laboratoire des Biotechnologies Microbiennes et Enzymatiques et de Biomol\u00e9cules (LBMEB), Centre de Biotechnologie de Sfax (CBS), Universit\u00e9 de Sfax (USF), Route de Sidi Mansour Km 6, BP 1177, Sfax 3018, Tunisia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ahlem","family":"Dab","sequence":"additional","affiliation":[{"name":"G\u00e9nie Enzymatique, Membranes Biomim\u00e9tiques et Assemblages Supramol\u00e9culaires (GEMBAS), Institut de Chimie et de Biochimie Mol\u00e9culaires et Supramol\u00e9culaires (ICBMS), UMR 5246 CNRS, Univ Lyon, Universit\u00e9 Lyon 1, B\u00e2t Raulin, 43 Bd du 11 Novembre 1918, F-69622 Villeurbanne cedex, France"},{"name":"Laboratoire des Biotechnologies Microbiennes et Enzymatiques et de Biomol\u00e9cules (LBMEB), Centre de Biotechnologie de Sfax (CBS), Universit\u00e9 de Sfax (USF), Route de Sidi Mansour Km 6, BP 1177, Sfax 3018, Tunisia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0587-2986","authenticated-orcid":false,"given":"Nour Eddine","family":"Bentouhami","sequence":"additional","affiliation":[{"name":"Laboratoire de Bioressources, Biotechnologie, Ethnopharmacologie et Sant\u00e9 (LBBES), Facult\u00e9 des Sciences d\u2019Oujda (FSO), Universit\u00e9 Mohammed Premier (UMP), Bd Mohamed VI BP 717, Oujda 60000, 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Chem. Biol."},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Pereira, M.G., Velasco-Lozano, S., Moreno-Perez, S., Polizeli, A.M., Heinen, P.R., Facchini, F.D.A., Vici, A.C., Cereia, M., Pessela, B.C., and Fernandez-Lorente, G. (2017). Different covalent immobilizations modulate lipase activities of Hypocrea pseudokoningii. Molecules, 22.","DOI":"10.3390\/molecules22091448"},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Chapman, J., Ismail, A.E., and Dinu, C.Z. (2018). Industrial applications of enzymes: Recent advances, techniques, and outlooks. Catalysts, 8.","DOI":"10.3390\/catal8060238"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"6653","DOI":"10.1080\/10408398.2022.2038076","article-title":"Sources, purification, immobilization and industrial applications of microbial lipases: An overview","volume":"63","author":"Enespa","year":"2022","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1080\/10408690390251147","article-title":"Lipase mediated upgradation of dietary fats and oils","volume":"43","author":"Gupta","year":"2003","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Bharathi, D., and Rajalakshmi, G. (2019). Microbial lipases: An overview of screening, production and purification. Biocatal. Agric. Biotechnol., 22.","DOI":"10.1016\/j.bcab.2019.101368"},{"key":"ref_7","first-page":"4836","article-title":"Enzymes Used in Detergents: Lipases","volume":"9","author":"Hasan","year":"2010","journal-title":"Afr. J. Biotechnol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/j.procbio.2024.03.005","article-title":"Production of structured lipids via batch and continuous acidolysis of triglycerides using the hydration\u2013aggregation-pretreated lipase loaded onto surface-modified glass bead supports","volume":"141","author":"Yoshioka","year":"2024","journal-title":"Process Biochem."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1080\/10242422.2023.2265019","article-title":"Zinc hydroxide salts as new supports for the immobilization of Pseudomonas cepacia lipase","volume":"42","author":"Dias","year":"2023","journal-title":"Biocatal. Biotransform."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.procbio.2024.02.017","article-title":"Isocyanate-mediated immobilization of Candida antarctica lipase B onto resin for efficient 1,3-diacylglycerol bio-synthesis","volume":"141","author":"Liang","year":"2024","journal-title":"Process Biochem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1689","DOI":"10.1080\/10408398.2020.1764489","article-title":"Immobilized microbial lipases in the food industry: A systematic literature review","volume":"61","author":"Coelho","year":"2021","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"ref_12","first-page":"274","article-title":"Immobilization of Rhizomucor miehei lipase onto montmorillonite K-10 and polyvinyl alcohol gel","volume":"38","author":"Yildirim","year":"2020","journal-title":"Biocatal. Biotransform."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"14139","DOI":"10.3390\/molecules190914139","article-title":"Inorganic materials as supports for covalent enzyme immobilization: Methods and mechanisms","volume":"19","author":"Zucca","year":"2014","journal-title":"Molecules"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"5500","DOI":"10.1002\/adsc.201900439","article-title":"Immobilization of enzymes in\/on membranes and their applications","volume":"361","author":"Cen","year":"2019","journal-title":"Adv. Synth. Catal."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"1326","DOI":"10.1016\/j.ijbiomac.2022.09.161","article-title":"Preparation, characterization, immobilization, and molecular docking analysis of a novel detergent-stable subtilisin-like serine protease from Streptomyces mutabilis strain TN-X30","volume":"222","author":"Mechri","year":"2022","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1080\/13102818.2015.1008192","article-title":"An overview of technologies for immobilization of enzymes and surface analysis techniques for immobilized enzymes","volume":"29","author":"Marzuki","year":"2015","journal-title":"Biotechnol. Biotechnol. Equip."},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Srivastava, M., Srivastava, N., Ramteke, P.W., and Mishra, P.K. (2019). Immobilization methods of enzymes: Part I. Approaches to Enhance Industrial Production of Fungal Cellulases, Springer International Publishing. Fungal Biology.","DOI":"10.1007\/978-3-030-14726-6"},{"key":"ref_18","first-page":"43","article-title":"Effect of calcination temperature of the kaolin and molar Na2O\/SiO2 activator ratio on physical and microstructural properties of metakaolin based geopolymers","volume":"9","author":"Soleimani","year":"2012","journal-title":"Iran. Mater. Sci. Eng."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.procbio.2022.01.004","article-title":"Applications of immobilized lipases in enzymatic reactors: A review","volume":"114","author":"Remonatto","year":"2022","journal-title":"Process Biochem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"4281","DOI":"10.1002\/jsfa.7641","article-title":"Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry","volume":"96","author":"Bezbradica","year":"2016","journal-title":"J. Sci. Food Agric."},{"key":"ref_21","unstructured":"Cavaco-Paulo, A., Nierstrasz, V.A., and Wang, Q. (2019). 6\u2014Enzyme stabilization for biotechnological applications. Advances in Textile Biotechnology, Woodhead Publishing. [2nd ed.]."},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Rivero, C.W., and Palomo, J.M. (2016). Covalent immobilization of Candida rugosa Lipase at Alkaline pH and Their Application in the Regioselective Deprotection of Per-O-Acetylated Thymidine. Catalysts, 6.","DOI":"10.3390\/catal6080115"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.procbio.2024.01.031","article-title":"Green synthesis of iron-alginate nanoparticle for taguchi-assisted immobilization of Candida rugosa lipase and its application in the synthesis of butyl butyrate ester","volume":"139","author":"Sharma","year":"2024","journal-title":"Process Biochem."},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Hasnaoui, I., Dab, A., Mechri, S., Abouloifa, H., Saalaoui, E., Jaouadi, B., Noiriel, A., Asehraou, A., and Abousalham, A. (2022). Purification, Biochemical and kinetic characterization of a novel alkaline sn-1,3-regioselective triacylglycerol lipase from Penicillium crustosum Thom strain P22 isolated from Moroccan olive mill wastewater. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms231911920"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1016\/j.bej.2007.03.006","article-title":"Immobilization studies and biochemical properties of free and immobilized Rhizopus oryzae lipase onto CaCO3: A comparative study","volume":"37","author":"Ghamgui","year":"2007","journal-title":"Biochem. Eng. J."},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Ben Bacha, A., Alonazi, M., Alanazi, H., Alharbi, M.G., Jallouli, R., and Karray, A. (2022). Biochemical study of Bacillus stearothermophilus immobilized lipase for oily wastewater treatment. Processes, 10.","DOI":"10.3390\/pr10112220"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"157","DOI":"10.5757\/ASCT.2017.26.6.157","article-title":"An overview of techniques in enzyme immobilization","volume":"26","author":"Nguyen","year":"2017","journal-title":"Appl. Sci. Converg. Technol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1002\/bit.260300112","article-title":"Rules for optimization of biocatalysis in organic Solvents","volume":"30","author":"Laane","year":"1987","journal-title":"Biotechnol. Bioeng."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1016\/j.ijbiomac.2021.02.028","article-title":"Evaluating enzyme stabilizations in calcium carbonate: Comparing in situ and crosslinking mediated immobilization","volume":"175","author":"Lee","year":"2021","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Adney, W.S., McMillan, J.D., Mielenz, J., and Klasson, K.T. (2008). Immobilization of Yarrowia lipolytica lipase\u2014A comparison of stability of physical adsorption and covalent attachment techniques. Biotechnology for Fuels and Chemicals. ABAB Symposium, Humana Press.","DOI":"10.1007\/978-1-60327-526-2"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1007\/s10295-011-1027-3","article-title":"Immobilization of Candida rugosa Lipase on Poly(3-Hydroxybutyrate-Co-Hydroxyvalerate): A New Eco-Friendly Support","volume":"39","author":"Lisboa","year":"2012","journal-title":"J. Ind. Microbiol. Biotechnol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"625258","DOI":"10.1155\/2014\/625258","article-title":"Organic solvent tolerant lipases and applications","volume":"2014","author":"Sharma","year":"2014","journal-title":"Sci. World J."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"2181","DOI":"10.5012\/bkcs.2012.33.7.2181","article-title":"Covalent immobilization of trypsin on a novel aldehyde-terminated PAMAM Dendrimer","volume":"33","author":"Hamidi","year":"2012","journal-title":"Bull. Korean Chem. Soc."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"2149","DOI":"10.1016\/j.procbio.2004.08.014","article-title":"Optimization of lipase entrapment in ca-alginate gel beads","volume":"40","author":"Won","year":"2005","journal-title":"Process Biochem."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/j.enzmictec.2015.10.005","article-title":"Lipase in biphasic alginate beads as a biocatalyst for esterification of butyric acid and butanol in aqueous media","volume":"82","author":"Ng","year":"2016","journal-title":"Enzyme Microb. Technol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"738739","DOI":"10.1155\/2014\/738739","article-title":"Immobilization of a plant lipase from Pachira aquatica in Alginate and Alginate\/PVA Beads","volume":"2014","author":"Bonine","year":"2014","journal-title":"Enzym. Res."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"10037","DOI":"10.1039\/D2NJ01160C","article-title":"Characterization of lipase from Candida rugosa entrapped in alginate beads to enhance its thermal stability and recyclability","volume":"46","author":"Vetrano","year":"2022","journal-title":"New J. Chem."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1080\/10826068.2022.2142799","article-title":"The response surface methodology for optimization of Halomonas sp. C2SS100 lipase immobilization onto CaCO3 for treatment of tuna wash processing wastewater","volume":"53","author":"Khmaissa","year":"2022","journal-title":"Preparative Biochem. Biotechnol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.bej.2015.12.019","article-title":"Accessing Regio-and Typo-Selectivity of Yarrowia lipolytica Lipase in its free form and immobilized onto magnetic nanoparticles","volume":"109","author":"Akil","year":"2016","journal-title":"Biochem. Eng. J."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1016\/j.ijbiomac.2018.05.156","article-title":"Interaction of Yarrowia lipolytica lipase with dithiocarbamate modified magnetic carbon Fe3O4@C-NHCS2H core-shell nanoparticles","volume":"117","author":"Fathi","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1002\/bbb.1719","article-title":"Biodiesel production using immobilized lipase: Feasibility and challenges","volume":"10","author":"Sankaran","year":"2016","journal-title":"Biofuels Bioprod. Biorefin."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1002\/bit.260390405","article-title":"Organic Solvents Strip Water off Enzymes","volume":"39","author":"Gorman","year":"1992","journal-title":"Biotechnol. Bioeng."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1002\/bbb.1727","article-title":"The use of alternative solvents in enzymatic biodiesel production: A review","volume":"11","author":"Taher","year":"2017","journal-title":"Biofuels Bioprod. Biorefin."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"989","DOI":"10.5650\/jos.ess19125","article-title":"Synthesis of Methyl Butyrate Catalyzed by Lipase from Aspergillus fumigatus","volume":"68","author":"Kaur","year":"2019","journal-title":"J. Oleo Sci."},{"key":"ref_45","unstructured":"Das, S., and Dash, H.R. (2019). Chapter 18\u2014Microbial community dynamics of extremophiles\/extreme environment. Microbial Diversity in the Genomic Era, Academic Press."},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Ramos, P.R., Kamimura, E.S., Pires, N.A.M., Maldonado, R.R., and de Oliveira, A.L. (2021). Esterification reaction in SC-CO2 catalyzed by lipase produced with corn steep liquor and minas frescal cheese whey. Bioresour. Technol. Rep., 14.","DOI":"10.1016\/j.biteb.2021.100670"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1007\/s12033-012-9518-7","article-title":"Gene cloning and characterization of a novel highly organic solvent tolerant lipase from Proteus sp. SW1 and Its application for biodiesel production","volume":"53","author":"Whangsuk","year":"2013","journal-title":"Mol. Biotechnol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/j.jbiotec.2008.10.004","article-title":"Development of recombinant E. coli whole-cell biocatalyst expressing a novel alkaline lipase-coding gene from Proteus sp. for biodiesel production","volume":"139","author":"Gao","year":"2009","journal-title":"J. Biotechnol."},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Godoy, C.A. (2017). New strategy for the immobilization of lipases on glyoxyl-agarose supports: Production of robust biocatalysts for natural oil transformation. Int. J. Mol. Sci., 18.","DOI":"10.3390\/ijms18102130"},{"key":"ref_50","first-page":"e1618085","article-title":"Investigating enzyme activity of immobilized Candida rugosa lipase","volume":"2018","author":"Lumor","year":"2018","journal-title":"J. Food Qual."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."}],"container-title":["Molecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1420-3049\/30\/3\/434\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,8]],"date-time":"2025-10-08T10:32:33Z","timestamp":1759919553000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1420-3049\/30\/3\/434"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,1,21]]},"references-count":51,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2025,2]]}},"alternative-id":["molecules30030434"],"URL":"https:\/\/doi.org\/10.3390\/molecules30030434","relation":{},"ISSN":["1420-3049"],"issn-type":[{"value":"1420-3049","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,1,21]]}}}