{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,28]],"date-time":"2026-06-28T05:29:02Z","timestamp":1782624542992,"version":"3.54.5"},"reference-count":125,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2024,12,1]],"date-time":"2024-12-01T00:00:00Z","timestamp":1733011200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,12,1]],"date-time":"2024-12-01T00:00:00Z","timestamp":1733011200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,9,18]],"date-time":"2024-09-18T00:00:00Z","timestamp":1726617600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100020884","name":"Agencia Nacional de Investigaci\u00f3n y Desarrollo","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100020884","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100009092","name":"Universidad de Alicante","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100009092","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100011033","name":"State Agency of Research","doi-asserted-by":"publisher","award":["PID2022-136535OB-I00"],"award-info":[{"award-number":["PID2022-136535OB-I00"]}],"id":[{"id":"10.13039\/501100011033","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002717","name":"Minist\u00e8re de l'Enseignement Sup\u00e9rieur et de la Recherche Scientifique","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002717","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004837","name":"Ministerio de Ciencia e Innovaci\u00f3n","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004837","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002850","name":"Fondo Nacional de Desarrollo Cient\u00edfico y Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["1231631"],"award-info":[{"award-number":["1231631"]}],"id":[{"id":"10.13039\/501100002850","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Enzyme and Microbial Technology"],"published-print":{"date-parts":[[2024,12]]},"DOI":"10.1016\/j.enzmictec.2024.110517","type":"journal-article","created":{"date-parts":[[2024,9,21]],"date-time":"2024-09-21T02:24:31Z","timestamp":1726885471000},"page":"110517","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":5,"special_numbering":"C","title":["Changes in ficin specificity by different substrate proteins promoted by enzyme immobilization"],"prefix":"10.1016","volume":"181","author":[{"given":"Alex D.","family":"Gonzalez-Vasquez","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"El Siar","family":"Hocine","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marcela","family":"Urz\u00faa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Javier","family":"Rocha-Martin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roberto","family":"Fernandez-Lafuente","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.enzmictec.2024.110517_bib1","doi-asserted-by":"crossref","DOI":"10.1016\/j.fbio.2024.103922","article-title":"Effects of rice bran stabilization procedures and proteases on rice bran protein hydrolysates","volume":"59","author":"Ouyang","year":"2024","journal-title":"Food Biosci."},{"key":"10.1016\/j.enzmictec.2024.110517_bib2","doi-asserted-by":"crossref","DOI":"10.1016\/j.jff.2024.106227","article-title":"Characterization and evaluation of the in vitro and in vivo anti-diabetic activities of camel milk protein hydrolysates derived with different protease digestions","volume":"117","author":"Yu","year":"2024","journal-title":"J. Funct. Foods"},{"key":"10.1016\/j.enzmictec.2024.110517_bib3","doi-asserted-by":"crossref","first-page":"1847","DOI":"10.1007\/s10068-023-01490-z","article-title":"Hydrolysates with emulsifying properties prepared from protein wastes using microbial protease","volume":"33","author":"Padmapriya","year":"2024","journal-title":"Food Sci. Biotechnol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib4","doi-asserted-by":"crossref","first-page":"1484","DOI":"10.1016\/j.foodchem.2008.11.049","article-title":"Enzymatic hydrolysis of hemp (Cannabis sativa L.) protein isolate by various proteases and antioxidant properties of the resulting hydrolysates","volume":"114","author":"Tang","year":"2009","journal-title":"Food Chem."},{"key":"10.1016\/j.enzmictec.2024.110517_bib5","first-page":"131","article-title":"Evaluation the effect of hydrolysis conditions and type of protease on the degree of hydrolysis and antioxidant properties of the protein hydrolysate from the skipjack fish (Katsuwonus pelamis) viscera by the response surface methodology","volume":"20","author":"Kaveh","year":"2024","journal-title":"J. Food Sci. Technol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib6","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1016\/j.biortech.2006.12.015","article-title":"Optimization of enzymatic hydrolysis of visceral waste proteins of Catla (Catla catla) for preparing protein hydrolysate using a commercial protease","volume":"99","author":"Bhaskar","year":"2008","journal-title":"Bioresour. Technol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib7","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.molcatb.2013.01.011","article-title":"Protein hydrolysis using proteases: an important tool for food biotechnology","volume":"90","author":"Tavano","year":"2013","journal-title":"J. Mol. Catal. B Enzym"},{"key":"10.1016\/j.enzmictec.2024.110517_bib8","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2024.130069","article-title":"Integrated extraction, structural characterization, and activity assessment of squid pen protein hydrolysates and \u03b2-chitin with different protease hydrolysis","volume":"262","author":"Li","year":"2024","journal-title":"Int J. Biol. Macromol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib9","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/j.foodres.2017.10.044","article-title":"Microbial proteases: production and application in obtaining protein hydrolysates","volume":"103","author":"dos Santos Aguilar","year":"2018","journal-title":"Food Res Int"},{"key":"10.1016\/j.enzmictec.2024.110517_bib10","doi-asserted-by":"crossref","first-page":"534","DOI":"10.1016\/j.chembiol.2023.09.009","article-title":"An N terminomics toolbox combining 2-pyridinecarboxaldehyde probes and click chemistry for profiling protease specificity","volume":"31","author":"Bridge","year":"2024","journal-title":"Cell Chem. Biol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib11","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1002\/pro.5560040301","article-title":"Structural basis of substrate specificity in the serine proteases","volume":"4","author":"Perona","year":"1995","journal-title":"Protein Sci."},{"key":"10.1016\/j.enzmictec.2024.110517_bib12","doi-asserted-by":"crossref","first-page":"12824","DOI":"10.1074\/jbc.M513331200","article-title":"Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique specificities","volume":"281","author":"Choe","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.enzmictec.2024.110517_bib13","doi-asserted-by":"crossref","first-page":"4501","DOI":"10.1021\/cr000033x","article-title":"serine protease mechanism and specificity","volume":"102","author":"Hedstrom","year":"2002","journal-title":"Chem. Rev."},{"key":"10.1016\/j.enzmictec.2024.110517_bib14","doi-asserted-by":"crossref","first-page":"7754","DOI":"10.1073\/pnas.140132697","article-title":"Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries","volume":"97","author":"Harris","year":"2000","journal-title":"P Natl. A Sci."},{"key":"10.1016\/j.enzmictec.2024.110517_bib15","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/S1074-5521(97)90258-1","article-title":"A combinatorial approach for determining protease specificities: application to interleukin-1\u03b2 converting enzyme (ICE)","volume":"4","author":"Rano","year":"1997","journal-title":"Chem. Biol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib16","doi-asserted-by":"crossref","first-page":"14868","DOI":"10.1021\/ja027477q","article-title":"Peptide Microarrays for the determination of protease substrate specificity","volume":"124","author":"Salisbury","year":"2002","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.enzmictec.2024.110517_bib17","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2303590120","article-title":"Prediction and design of protease enzyme specificity using a structure-aware graph convolutional network","volume":"120","author":"Lu","year":"2023","journal-title":"P Natl. A Sci."},{"key":"10.1016\/j.enzmictec.2024.110517_bib18","doi-asserted-by":"crossref","DOI":"10.1016\/j.jclepro.2023.138915","article-title":"Importance of enzyme specificity and stability for the application of proteases in greener industrial processing- a review","volume":"425","author":"Sujitha","year":"2023","journal-title":"J. Clean. Prod."},{"key":"10.1016\/j.enzmictec.2024.110517_bib19","doi-asserted-by":"crossref","first-page":"9956","DOI":"10.1038\/s41598-022-13617-z","article-title":"Reengineering the specificity of the highly selective Clostridium botulinum protease via directed evolution","volume":"12","author":"Dyer","year":"2022","journal-title":"Sci. Rep."},{"key":"10.1016\/j.enzmictec.2024.110517_bib20","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodchem.2020.128765","article-title":"Physicochemical properties and antioxidant activities of tree peony (Paeonia suffruticosa Andr.) seed protein hydrolysates obtained with different proteases","volume":"345","author":"Wang","year":"2021","journal-title":"Food Chem."},{"key":"10.1016\/j.enzmictec.2024.110517_bib21","doi-asserted-by":"crossref","first-page":"1718","DOI":"10.1002\/jsfa.5957","article-title":"Antioxidant activity of protein hydrolysates from whole anchovy sprat (Clupeonella engrauliformis) prepared using endogenous enzymes and commercial proteases","volume":"93","author":"Ovissipour","year":"2013","journal-title":"J. Sci. Food Agric."},{"key":"10.1016\/j.enzmictec.2024.110517_bib22","doi-asserted-by":"crossref","first-page":"1027","DOI":"10.3390\/ijms17071027","article-title":"Use of different proteases to obtain flaxseed protein hydrolysates with antioxidant activity","volume":"17","author":"Karama\u0107","year":"2016","journal-title":"Int J. Mol. Sci."},{"key":"10.1016\/j.enzmictec.2024.110517_bib23","doi-asserted-by":"crossref","DOI":"10.1016\/j.fbio.2019.100450","article-title":"Antioxidant, anticancer and ACE-inhibitory activities of bioactive peptides from wheat germ protein hydrolysates","volume":"32","author":"Karami","year":"2019","journal-title":"Food Biosci."},{"key":"10.1016\/j.enzmictec.2024.110517_bib24","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1007\/s11130-016-0576-z","article-title":"Antioxidant and anticancer activities of walnut (Juglans regia L.) protein hydrolysates using different proteases","volume":"71","author":"Jahanbani","year":"2016","journal-title":"Plant Foods Hum. Nutr."},{"key":"10.1016\/j.enzmictec.2024.110517_bib25","doi-asserted-by":"crossref","first-page":"6437","DOI":"10.1039\/c3cs35506c","article-title":"Industrial use of immobilized enzymes","volume":"42","author":"Di Cosimo","year":"2013","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.enzmictec.2024.110517_bib26","doi-asserted-by":"crossref","first-page":"6236","DOI":"10.1039\/c3cs35511j","article-title":"Evaluation of immobilized enzymes for industrial applications","volume":"42","author":"Liese","year":"2013","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.enzmictec.2024.110517_bib27","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. Soc. Rev."},{"key":"10.1016\/j.enzmictec.2024.110517_bib28","doi-asserted-by":"crossref","first-page":"1148","DOI":"10.1111\/all.15678","article-title":"Protease allergens as initiators\u2013regulators of allergic inflammation","volume":"78","author":"Soh","year":"2023","journal-title":"Allergy"},{"key":"10.1016\/j.enzmictec.2024.110517_bib29","doi-asserted-by":"crossref","DOI":"10.3389\/falgy.2023.1265049","article-title":"Sensing of protease activity as a triggering mechanism of Th2 cell immunity and allergic disease","volume":"4","author":"Meloun","year":"2023","journal-title":"Front. Allergy"},{"key":"10.1016\/j.enzmictec.2024.110517_bib30","doi-asserted-by":"crossref","DOI":"10.1183\/16000617.0126-2023","article-title":"Airborne indoor allergen serine proteases and their contribution to sensitisation and activation of innate immunity in allergic airway disease","volume":"33","author":"Ouyang","year":"2024","journal-title":"Eur. Respir. Rev."},{"key":"10.1016\/j.enzmictec.2024.110517_bib31","doi-asserted-by":"crossref","first-page":"2852","DOI":"10.3390\/foods12152852","article-title":"comparative analysis of the immune response and the clinical allergic reaction to papain-like cysteine proteases from fig, kiwifruit, papaya, pineapple and mites in an Italian population","volume":"12","author":"Giangrieco","year":"2023","journal-title":"Foods"},{"key":"10.1016\/j.enzmictec.2024.110517_bib32","doi-asserted-by":"crossref","first-page":"682","DOI":"10.1016\/j.ijbiomac.2022.04.224","article-title":"A review on the immobilization of pepsin: A Lys-poor enzyme that is unstable at alkaline pH values","volume":"210","author":"Morellon-Sterling","year":"2022","journal-title":"Int J. Biol. Macromol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib33","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2024.133089","article-title":"A review on the immobilization of bromelain","volume":"273","author":"Tacias-Pascacio","year":"2024","journal-title":"Int J. Biol. Macromol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib34","doi-asserted-by":"crossref","first-page":"2885","DOI":"10.1002\/adsc.201100534","article-title":"Potential of different enzyme immobilization strategies to improve enzyme performance","volume":"353","author":"Garcia-Galan","year":"2011","journal-title":"Adv. Synth. Catal."},{"key":"10.1016\/j.enzmictec.2024.110517_bib35","doi-asserted-by":"crossref","first-page":"6251","DOI":"10.1039\/D2CS00083K","article-title":"Is enzyme immobilization a mature discipline? Some critical considerations to capitalize on the benefits of immobilization","volume":"51","author":"Bolivar","year":"2022","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.enzmictec.2024.110517_bib36","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.ijbiomac.2021.08.016","article-title":"Immobilization of papain: a review","volume":"188","author":"Tacias-Pascacio","year":"2021","journal-title":"Int J. Biol. Macromol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib37","doi-asserted-by":"crossref","first-page":"6290","DOI":"10.1039\/C2CS35231A","article-title":"Modifying enzyme activity and selectivity by immobilization","volume":"42","author":"Rodrigues","year":"2013","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.enzmictec.2024.110517_bib38","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/0167-7799(93)90057-G","article-title":"Mechanism-based strategies for protein thermostabilization","volume":"11","author":"Mozhaev","year":"1993","journal-title":"Trends Biotechnol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib39","doi-asserted-by":"crossref","first-page":"6534","DOI":"10.1039\/c3cs60137d","article-title":"Stabilizing biocatalysts","volume":"42","author":"Bommarius","year":"2013","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.enzmictec.2024.110517_bib40","doi-asserted-by":"crossref","first-page":"1451","DOI":"10.1016\/j.enzmictec.2007.01.018","article-title":"Improvement of enzyme activity, stability and selectivity via immobilization techniques","volume":"40","author":"Mateo","year":"2007","journal-title":"Enzym. Micro Technol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib41","first-page":"1","article-title":"Stabilization of enzymes against thermal inactivation","author":"Klibanov","year":"1983","journal-title":"Adv. Appl. Microbiol 29"},{"key":"10.1016\/j.enzmictec.2024.110517_bib42","doi-asserted-by":"crossref","first-page":"1019","DOI":"10.1016\/j.procbio.2008.06.004","article-title":"Enzyme stability and stabilization\u2014aqueous and non-aqueous environment","volume":"43","author":"Iyer","year":"2008","journal-title":"Process Biochem"},{"key":"10.1016\/j.enzmictec.2024.110517_bib43","doi-asserted-by":"crossref","first-page":"2823","DOI":"10.1021\/cs400684x","article-title":"Strategies for stabilization of enzymes in organic solvents","volume":"3","author":"Stepankova","year":"2013","journal-title":"ACS Catal."},{"key":"10.1016\/j.enzmictec.2024.110517_bib44","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0003-2697(79)80110-4","article-title":"Enzyme stabilization by immobilization","volume":"93","author":"Klibanov","year":"1979","journal-title":"Anal. Biochem"},{"key":"10.1016\/j.enzmictec.2024.110517_bib45","doi-asserted-by":"crossref","first-page":"8995","DOI":"10.3390\/molecules19078995","article-title":"Immobilization as a strategy for improving enzyme properties- Application to oxidoreductases","volume":"19","author":"Guzik","year":"2014","journal-title":"Molecules"},{"key":"10.1016\/j.enzmictec.2024.110517_bib46","first-page":"1","article-title":"The principles of enzyme stabilization I. Increase in thermostability of enzymes covalently bound to a complementary surface of a polymer support in a multipoint fashion","volume":"485","author":"Martinek","year":"1977","journal-title":"BBA-Enzymol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib47","doi-asserted-by":"crossref","first-page":"3336","DOI":"10.1002\/anie.200301664","article-title":"immobilizing enzymes: How to create more suitable\u2009biocatalysts","volume":"42","author":"Bornscheuer","year":"2003","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.enzmictec.2024.110517_bib48","doi-asserted-by":"crossref","first-page":"1232","DOI":"10.3390\/ijms14011232","article-title":"From protein engineering to immobilization: Promising strategies for the upgrade of industrial enzymes","volume":"14","author":"Singh","year":"2013","journal-title":"Int J. Mol. Sci."},{"key":"10.1016\/j.enzmictec.2024.110517_bib49","doi-asserted-by":"crossref","DOI":"10.1016\/j.biotechadv.2021.107821","article-title":"Stabilization of enzymes via immobilization: multipoint covalent attachment and other stabilization strategies","volume":"52","author":"Rodrigues","year":"2021","journal-title":"Biotechnol. Adv."},{"key":"10.1016\/j.enzmictec.2024.110517_bib50","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1016\/j.procbio.2017.04.009","article-title":"Stabilization of ficin extract by immobilization on glyoxyl agarose. Preliminary characterization of the biocatalyst performance in hydrolysis of proteins","volume":"58","author":"Siar","year":"2017","journal-title":"Process Biochem"},{"key":"10.1016\/j.enzmictec.2024.110517_bib51","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1016\/j.ijbiomac.2019.04.123","article-title":"Amination of ficin extract to improve its immobilization on glyoxyl-agarose: improved stability and activity versus casein","volume":"133","author":"Siar","year":"2019","journal-title":"Int J. Biol. Macromol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib52","doi-asserted-by":"crossref","first-page":"676","DOI":"10.3390\/catal10060676","article-title":"high stabilization of enzymes immobilized on rigid hydrophobic glyoxyl-supports: generation of hydrophilic environments on support surfaces","volume":"10","author":"H. Orrego","year":"2020","journal-title":"Catalysts"},{"key":"10.1016\/j.enzmictec.2024.110517_bib53","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1016\/j.procbio.2010.12.007","article-title":"Lipase B from Candida antarctica immobilized on octadecyl sepabeads: a very stable biocatalyst in the presence of hydrogen peroxide","volume":"46","author":"Hernandez","year":"2011","journal-title":"Process Biochem"},{"key":"10.1016\/j.enzmictec.2024.110517_bib54","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/S1381-1177(99)00040-5","article-title":"Stabilization of enzymes (D-amino acid oxidase) against hydrogen peroxide via immobilization and post-immobilization techniques","volume":"7","author":"Fern\u00e1ndez-Lafuente","year":"1999","journal-title":"J. Mol. Catal. B Enzym"},{"key":"10.1016\/j.enzmictec.2024.110517_bib55","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/S0141-0229(98)00102-1","article-title":"Facile synthesis of artificial enzyme nano-environments via solid-phase chemistry of immobilized derivatives: dramatic stabilization of penicillin acylase versus organic solvents","volume":"24","author":"Fernandez-Lafuente","year":"1999","journal-title":"Enzym. Micro Technol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib56","article-title":"Uricase alkaline enzymosomes with enhanced stabilities and anti-hyperuricemia effects induced by favorable microenvironmental changes","volume":"6","author":"Zhou","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.enzmictec.2024.110517_bib57","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1007\/s12257-009-0188-7","article-title":"Post-immobilization of modified macromolecular reagents using assembled penicillin acylase for microenvironmental regulation of nanopores and enhancement of enzyme stability","volume":"15","author":"Zhou","year":"2010","journal-title":"Biotechnol. Bioproc. Eng."},{"key":"10.1016\/j.enzmictec.2024.110517_bib58","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1016\/j.enzmictec.2009.08.009","article-title":"Stabilization of multimeric enzymes: Strategies to prevent subunit dissociation","volume":"45","author":"Fernandez-Lafuente","year":"2009","journal-title":"Enzym. Micro Technol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib59","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.enzmictec.2015.02.001","article-title":"Immobilization of lipases on hydrophobic supports involves the open form of the enzyme","volume":"71","author":"Manoel","year":"2015","journal-title":"Enzym. Micro Technol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib60","doi-asserted-by":"crossref","first-page":"746","DOI":"10.1016\/j.biotechadv.2019.04.003","article-title":"Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions","volume":"37","author":"Rodrigues","year":"2019","journal-title":"Biotechnol. Adv."},{"key":"10.1016\/j.enzmictec.2024.110517_bib61","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1016\/j.biotechadv.2015.03.006","article-title":"Strategies for the one-step immobilization\u2013purification of enzymes as industrial biocatalysts","volume":"33","author":"Barbosa","year":"2015","journal-title":"Biotechnol. Adv."},{"key":"10.1016\/j.enzmictec.2024.110517_bib62","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1002\/jctb.6876","article-title":"Polypropylene as a selective support for the immobilization of lipolytic enzymes: hyper-activation, purification and biotechnological applications","volume":"97","author":"S\u00e1nchez-Otero","year":"2022","journal-title":"J. Chem. Technol. Biot."},{"key":"10.1016\/j.enzmictec.2024.110517_bib63","doi-asserted-by":"crossref","DOI":"10.1016\/j.seppur.2022.122758","article-title":"One-step purification of target enzymes using interaction- and structure-based design of aptamer-affinity responsive polymers: Selective immobilization and enhanced stability","volume":"307","author":"Wang","year":"2023","journal-title":"Sep Purif. Technol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib64","doi-asserted-by":"crossref","first-page":"364","DOI":"10.1002\/elsc.202000093","article-title":"One-step selective affinity purification and immobilization of His-tagged enzyme by recyclable magnetic nanoparticles","volume":"21","author":"Zhou","year":"2021","journal-title":"Eng. Life Sci."},{"key":"10.1016\/j.enzmictec.2024.110517_bib65","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1007\/s11274-023-03796-w","article-title":"Tyrosinase enzyme purification and immobilization from Pseudomonas sp. EG22 using cellulose coated magnetic nanoparticles: characterization and application in melanin production","volume":"40","author":"El-Aziz","year":"2024","journal-title":"World J. Microbiol Biotechnol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib66","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-023-48795-x","article-title":"Direct purification and immobilization of his-tagged enzymes using unmodified nickel ferrite NiFe2O4 magnetic nanoparticles","volume":"13","author":"Lau","year":"2023","journal-title":"Sci. Rep."},{"key":"10.1016\/j.enzmictec.2024.110517_bib67","doi-asserted-by":"crossref","first-page":"3864","DOI":"10.3390\/ijms24043864","article-title":"selective immobilization of his-tagged enzyme on Ni-chelated ion exchange resin and its application in protein purification","volume":"24","author":"Wang","year":"2023","journal-title":"Int J. Mol. Sci."},{"key":"10.1016\/j.enzmictec.2024.110517_bib68","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodchem.2019.125037","article-title":"One-step immobilization-purification of enzymes by carbohydrate-binding module family 56 tag fusion","volume":"299","author":"Qin","year":"2019","journal-title":"Food Chem."},{"key":"10.1016\/j.enzmictec.2024.110517_bib69","doi-asserted-by":"crossref","first-page":"31878","DOI":"10.1021\/acsami.9b09071","article-title":"novel synthesis strategy for biocatalyst: fast purification and immobilization of His- and ELP-tagged enzyme from fermentation broth","volume":"11","author":"Zhao","year":"2019","journal-title":"ACS Appl. Mater. Inter"},{"key":"10.1016\/j.enzmictec.2024.110517_bib70","doi-asserted-by":"crossref","DOI":"10.3389\/fbioe.2020.00579","article-title":"immobilization and purification of enzymes with the novel affinity tag ChBD-AB from Chitinolyticbacter meiyuanensis SYBC-H1","volume":"8","author":"Zhou","year":"2020","journal-title":"Front Bioeng. Biotechnol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib71","doi-asserted-by":"crossref","first-page":"3034","DOI":"10.1038\/ncomms4034","article-title":"Dynamic heterogeneity controls diffusion and viscosity near biological interfaces","volume":"5","author":"Pronk","year":"2014","journal-title":"Nat. Commun."},{"key":"10.1016\/j.enzmictec.2024.110517_bib72","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1002\/bit.260160808","article-title":"Influence of intraparticle diffusional limitation on the observed kinetics of immobilized enzymes and on catalyst design","volume":"16","author":"Regan","year":"1974","journal-title":"Biotechnol. Bioeng."},{"key":"10.1016\/j.enzmictec.2024.110517_bib73","doi-asserted-by":"crossref","first-page":"3748","DOI":"10.1016\/j.ces.2007.03.041","article-title":"Critical review of the impact of tortuosity on diffusion","volume":"62","author":"Shen","year":"2007","journal-title":"Chem. Eng. Sci."},{"key":"10.1016\/j.enzmictec.2024.110517_bib74","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1016\/j.tibtech.2013.01.004","article-title":"Shine a light on immobilized enzymes: real-time sensing in solid supported biocatalysts","volume":"31","author":"Bolivar","year":"2013","journal-title":"Trends Biotechnol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib75","doi-asserted-by":"crossref","first-page":"3674","DOI":"10.3390\/molecules29153674","article-title":"Support enzyme loading affects the effect of the immobilized ficin modification with aldehyde dextran on the specificity for large proteins","volume":"29","author":"Siar","year":"2024","journal-title":"Molecules"},{"key":"10.1016\/j.enzmictec.2024.110517_bib76","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.jbiotec.2024.09.005","article-title":"Designing tailor-made steric matters to improve the immobilized ficin specificity for small versus large proteins","volume":"395","author":"Siar","year":"2024","journal-title":"J. Biotechnol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib77","doi-asserted-by":"crossref","first-page":"6250","DOI":"10.1039\/c3cs35495d","article-title":"Conformational changes of enzymes upon immobilisation","volume":"42","author":"Secundo","year":"2013","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.enzmictec.2024.110517_bib78","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1016\/S0141-0229(00)00324-0","article-title":"Modulation of lipase properties in macro-aqueous systems by controlled enzyme immobilization: enantioselective hydrolysis of a chiral ester by immobilized Pseudomonas lipase","volume":"28","author":"Fern\u00e1ndez-Lorente","year":"2001","journal-title":"Enzym. Micro Technol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib79","doi-asserted-by":"crossref","first-page":"36","DOI":"10.3389\/fbioe.2020.00036","article-title":"Effects of enzyme loading and immobilization conditions on the catalytic features of lipase from Pseudomonas fluorescens immobilized on octyl-agarose beads","volume":"8","author":"Arana-Pe\u00f1a","year":"2020","journal-title":"Front Bioeng. Biotechnol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib80","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1016\/j.procbio.2016.04.002","article-title":"Easy stabilization of interfacially activated lipases using heterofunctional divinyl sulfone activated-octyl agarose beads. Modulation of the immobilized enzymes by altering their nanoenvironment","volume":"51","author":"Albuquerque","year":"2016","journal-title":"Process Biochem"},{"key":"10.1016\/j.enzmictec.2024.110517_bib81","doi-asserted-by":"crossref","first-page":"1272","DOI":"10.1021\/ja3120136","article-title":"A New Nanobiocatalytic system based on allosteric effect with dramatically enhanced enzymatic performance","volume":"135","author":"Wang","year":"2013","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.enzmictec.2024.110517_bib82","doi-asserted-by":"crossref","first-page":"3717","DOI":"10.1021\/am5084545","article-title":"Modulating the activity of protein conjugated to gold nanoparticles by site-directed orientation and surface density of bound protein","volume":"7","author":"Liu","year":"2015","journal-title":"ACS Appl. Mater. Inter"},{"key":"10.1016\/j.enzmictec.2024.110517_bib83","article-title":"Surfactant-activated lipase hybrid nanoflowers with enhanced enzymatic performance","volume":"6","author":"Cui","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.enzmictec.2024.110517_bib84","doi-asserted-by":"crossref","first-page":"562","DOI":"10.1039\/b517104k","article-title":"Immobilization of lipase on silicas. Relevance of textural and interfacial properties on activity and selectivity","volume":"30","author":"Galarneau","year":"2006","journal-title":"New J. Chem."},{"key":"10.1016\/j.enzmictec.2024.110517_bib85","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0133857","article-title":"immobilization, regiospecificity characterization and application of Aspergillus oryzae lipase in the enzymatic synthesis of the structured lipid 1,3-dioleoyl-2-palmitoylglycerol","volume":"10","author":"Cai","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.enzmictec.2024.110517_bib86","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.molcatb.2011.03.007","article-title":"Improving catalytic performance of Burkholderia cepacia lipase immobilized on macroporous resin NKA","volume":"71","author":"Liu","year":"2011","journal-title":"J. Mol. Catal. B Enzym"},{"key":"10.1016\/j.enzmictec.2024.110517_bib87","doi-asserted-by":"crossref","first-page":"1833","DOI":"10.1016\/j.ijbiomac.2018.07.030","article-title":"Enzymes and nanoparticles: Modulation of enzymatic activity via nanoparticles","volume":"118","author":"Arsalan","year":"2018","journal-title":"Int J. Biol. Macromol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib88","doi-asserted-by":"crossref","first-page":"674","DOI":"10.1016\/j.ijbiomac.2017.12.062","article-title":"Immobilization of lipases in hydrophobic chitosan for selective hydrolysis of fish oil: The impact of support functionalization on lipase activity, selectivity and stability","volume":"108","author":"Urrutia","year":"2018","journal-title":"Int J. Biol. Macromol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib89","doi-asserted-by":"crossref","first-page":"3047","DOI":"10.1021\/bm070374l","article-title":"Lipolytic enzymes with improved activity and selectivity upon adsorption on polymeric nanoparticles","volume":"8","author":"Palocci","year":"2007","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.enzmictec.2024.110517_bib90","doi-asserted-by":"crossref","first-page":"8877","DOI":"10.1021\/la801384c","article-title":"Immobilization of lipases on hydrophobilized zirconia nanoparticles: highly enantioselective and reusable biocatalysts","volume":"24","author":"Chen","year":"2008","journal-title":"Langmuir"},{"key":"10.1016\/j.enzmictec.2024.110517_bib91","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1016\/j.ijbiomac.2020.06.144","article-title":"Ficin: a protease extract with relevance in biotechnology and biocatalysis","volume":"162","author":"Morellon-Sterling","year":"2020","journal-title":"Int J. Biol. Macromol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib92","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1021\/ed041p53","article-title":"Ficin as a catalyst in organic syntheses","volume":"31","author":"Abernethy","year":"1964","journal-title":"J. Chem. Educ."},{"key":"10.1016\/j.enzmictec.2024.110517_bib93","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1111\/j.1365-2621.2003.tb14119.x","article-title":"Effect of chemically modified soy proteins and ficin-tenderized meat on the quality attributes of sausage","volume":"68","author":"Ramezani","year":"2003","journal-title":"J. Food Sci."},{"key":"10.1016\/j.enzmictec.2024.110517_bib94","first-page":"158","article-title":"Enzyme activity of ficin preparations from different sources and their effect on meat","volume":"7","author":"Solov\u2019ev","year":"1973","journal-title":"Appl. Biochem Microbiol"},{"key":"10.1016\/j.enzmictec.2024.110517_bib95","first-page":"124","article-title":"Changes in the myofibrillar proteins of buffalo meat during its ripening and under the influence of ficin","volume":"8","year":"1974","journal-title":"Appl. Biochem Microbiol"},{"key":"10.1016\/j.enzmictec.2024.110517_bib96","doi-asserted-by":"crossref","first-page":"233","DOI":"10.3168\/jdsc.2020-0073","article-title":"Potential applications of ficin in the production of traditional cheeses and protein hydrolysates","volume":"2","author":"Aider","year":"2021","journal-title":"JDS Commun."},{"key":"10.1016\/j.enzmictec.2024.110517_bib97","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1002\/fsn3.553","article-title":"Rheological and structural properties of enzyme-induced gelation of milk proteins by ficin and Polyporus badius","volume":"6","author":"Shabani","year":"2018","journal-title":"Food Sci. Nutr."},{"key":"10.1016\/j.enzmictec.2024.110517_bib98","doi-asserted-by":"crossref","first-page":"4091","DOI":"10.3390\/molecules25184091","article-title":"Production and characterization of antioxidative hydrolysates and peptides from corn gluten meal using papain, ficin, and bromelain","volume":"25","author":"Hu","year":"2020","journal-title":"Molecules"},{"key":"10.1016\/j.enzmictec.2024.110517_bib99","doi-asserted-by":"crossref","first-page":"8467","DOI":"10.1039\/D3FO01408H","article-title":"Germinated chickpea protein ficin hydrolysate and its peptides inhibited glucose uptake and affected the bitter receptor signaling pathway in vitro","volume":"14","author":"Chandrasekaran","year":"2023","journal-title":"Food Funct."},{"key":"10.1016\/j.enzmictec.2024.110517_bib100","doi-asserted-by":"crossref","DOI":"10.1016\/j.fbio.2022.101707","article-title":"Functional properties of peptides obtained from whey proteins by ficin extract hydrolysis","volume":"47","author":"Kheroufi","year":"2022","journal-title":"Food Biosci."},{"key":"10.1016\/j.enzmictec.2024.110517_bib101","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodchem.2021.131717","article-title":"Optimization, identification, and comparison of peptides from germinated chickpea (Cicer arietinum) protein hydrolysates using either papain or ficin and their relationship with markers of type 2 diabetes","volume":"374","author":"Chandrasekaran","year":"2022","journal-title":"Food Chem."},{"key":"10.1016\/j.enzmictec.2024.110517_bib102","first-page":"523","article-title":"Study of the proteolytic activity of ficin associates with chitosan nanoparticles","volume":"24","author":"Olshannikova","year":"2022","journal-title":"Cond. Mat. Inter"},{"key":"10.1016\/j.enzmictec.2024.110517_bib103","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1107\/S2053230X15005014","article-title":"Crystallization and preliminary X-ray analysis of four cysteine proteases from Ficus carica latex","volume":"71","author":"Haesaerts","year":"2015","journal-title":"Acta Crystallogr F. Struct. Biol. Commun."},{"key":"10.1016\/j.enzmictec.2024.110517_bib104","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.phytochem.2012.12.006","article-title":"Purification and autolysis of the ficin isoforms from fig (Ficus carica cv. Sabz) latex","volume":"87","author":"Zare","year":"2013","journal-title":"Phytochemistry"},{"key":"10.1016\/j.enzmictec.2024.110517_bib105","doi-asserted-by":"crossref","first-page":"576","DOI":"10.1002\/jsfa.7126","article-title":"Characterisation of general proteolytic, milk clotting and antifungal activity of Ficus carica latex during fruit ripening","volume":"96","author":"Raskovic","year":"2016","journal-title":"J. Sci. Food Agric."},{"key":"10.1016\/j.enzmictec.2024.110517_bib106","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/j.ijbiomac.2019.12.140","article-title":"Use of glyoxyl-agarose immobilized ficin extract in milk coagulation: unexpected importance of the ficin loading on the biocatalysts","volume":"144","author":"Siar","year":"2020","journal-title":"Int J. Biol. Macromol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib107","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1016\/j.jbiotec.2021.02.005","article-title":"Effect of amine length in the interference of the multipoint covalent immobilization of enzymes on glyoxyl agarose beads","volume":"329","author":"Morellon-Sterling","year":"2021","journal-title":"J. Biotechnol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib108","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/j.procbio.2023.07.029","article-title":"Glyoxyl-ficin: an example where a more intense multipoint covalent attachment may decrease enzyme stability","volume":"132","author":"Siar","year":"2023","journal-title":"Process Biochem"},{"key":"10.1016\/j.enzmictec.2024.110517_bib109","unstructured":"A. Gonz\u00e1lez-V\u00e1squez, E.H. Siar, A. Alc\u00e1ntara R, M. Urz\u00faa, J. Rocha-Martin, R. Fernandez-Lafuente, Designing mixed cationic\/anionic supports to covalently immobilize\/stabilize enzymes with high isoelectric point by the enzyme adsorption and support-enzyme glutaraldehyde crosslinking method, Int J Biol Macromol Accepted pending revision."},{"key":"10.1016\/j.enzmictec.2024.110517_bib110","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.jbiotec.2005.05.021","article-title":"Enzyme stabilization by glutaraldehyde crosslinking of adsorbed proteins on aminated supports","volume":"119","author":"L\u00f3pez-Gallego","year":"2005","journal-title":"J. Biotechnol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib111","doi-asserted-by":"crossref","first-page":"1583","DOI":"10.1039\/C3RA45991H","article-title":"Glutaraldehyde in bio-catalysts design: a useful crosslinker and a versatile tool in enzyme immobilization","volume":"4","author":"Barbosa","year":"2014","journal-title":"RSC Adv."},{"key":"10.1016\/j.enzmictec.2024.110517_bib112","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1016\/0141-0229(94)00090-E","article-title":"Strategies for enzyme stabilization by intramolecular crosslinking with bifunctional reagents","volume":"17","author":"Fernandez-Lafuente","year":"1995","journal-title":"Enzym. Micro Technol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib113","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1016\/0304-5102(78)80026-1","article-title":"Optimization of glutaraldehyde activation of a support for enzyme immobilization","volume":"3","author":"Monsan","year":"1978","journal-title":"J. Mol. Catal."},{"key":"10.1016\/j.enzmictec.2024.110517_bib114","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1146\/annurev-food-022811-101214","article-title":"The structure of the casein micelle of milk and its changes during processing","volume":"3","author":"Dalgleish","year":"2012","journal-title":"Annu Rev. Food Sci. Technol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib115","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1016\/S1359-0294(02)00082-1","article-title":"Casein structure, self-assembly and gelation","volume":"7","author":"Horne","year":"2002","journal-title":"Curr. Opin. Colloid Interface Sci."},{"key":"10.1016\/j.enzmictec.2024.110517_bib116","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/S0958-6946(98)00040-5","article-title":"Casein interactions: casting light on the black boxes, the structure in dairy products","volume":"8","author":"Horne","year":"1998","journal-title":"Int Dairy J."},{"key":"10.1016\/j.enzmictec.2024.110517_bib117","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1039\/C4AN01495B","article-title":"Probing the secondary structure of bovine serum albumin during heat-induced denaturation using mid-infrared fiberoptic sensors","volume":"140","author":"Lu","year":"2015","journal-title":"Analyst"},{"key":"10.1016\/j.enzmictec.2024.110517_bib118","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1016\/j.molimm.2012.05.011","article-title":"Structural and immunologic characterization of bovine, horse, and rabbit serum albumins","volume":"52","author":"Majorek","year":"2012","journal-title":"Mol. Immunol."},{"key":"10.1016\/j.enzmictec.2024.110517_bib119","doi-asserted-by":"crossref","DOI":"10.1016\/j.talanta.2019.120317","article-title":"Latest developments in the detection and separation of bovine serum albumin using molecularly imprinted polymers","volume":"207","author":"Jahanban-Esfahlan","year":"2020","journal-title":"Talanta"},{"key":"10.1016\/j.enzmictec.2024.110517_bib120","doi-asserted-by":"crossref","first-page":"608","DOI":"10.1016\/0006-3002(58)90108-2","article-title":"Studies on the structure of hemoglobin I. Physicochemical properties of human globin","volume":"30","author":"Fanelli","year":"1958","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.enzmictec.2024.110517_bib121","doi-asserted-by":"crossref","first-page":"416","DOI":"10.1038\/185416a0","article-title":"Structure of H\u00e6moglobin: a three-dimensional Fourier synthesis at 5.5-\u00c5. resolution, obtained by X-ray analysis","volume":"185","author":"Perutz","year":"1960","journal-title":"Nature"},{"key":"10.1016\/j.enzmictec.2024.110517_bib122","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.procbio.2019.11.026","article-title":"Parameters necessary to define an immobilized enzyme preparation","volume":"90","author":"Boudrant","year":"2020","journal-title":"Process Biochem."},{"key":"10.1016\/j.enzmictec.2024.110517_bib123","article-title":"Influence of natural organic matter on the aggregation dynamics of biochar colloids derived from various feedstocks","volume":"46","author":"Li","year":"2024","journal-title":"SciTotal Envir"},{"key":"10.1016\/j.enzmictec.2024.110517_bib124","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodchem.2020.128108","article-title":"Glycation from \u03b1-dicarbonyl compounds has different effects on the heat-induced aggregation of bovine serum albumin and \u03b2-casein","volume":"340","author":"Zhao","year":"2021","journal-title":"Food Chem."},{"key":"10.1016\/j.enzmictec.2024.110517_bib125","doi-asserted-by":"crossref","DOI":"10.1016\/j.molstruc.2024.138226","article-title":"Clarifying the role of carboxyl functionality in squaraines towards aggregation and self-assembly through photophysical characterization and BSA interactions","volume":"1309","author":"Mavileti","year":"2024","journal-title":"J. Mol. Struct."}],"container-title":["Enzyme and Microbial Technology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141022924001248?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141022924001248?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,4,29]],"date-time":"2026-04-29T16:22:58Z","timestamp":1777479778000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0141022924001248"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,12]]},"references-count":125,"alternative-id":["S0141022924001248"],"URL":"https:\/\/doi.org\/10.1016\/j.enzmictec.2024.110517","relation":{},"ISSN":["0141-0229"],"issn-type":[{"value":"0141-0229","type":"print"}],"subject":[],"published":{"date-parts":[[2024,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Changes in ficin specificity by different substrate proteins promoted by enzyme immobilization","name":"articletitle","label":"Article Title"},{"value":"Enzyme and Microbial Technology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.enzmictec.2024.110517","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 The Author(s). Published by Elsevier Inc.","name":"copyright","label":"Copyright"}],"article-number":"110517"}}