Parameters necessary to define an immobilized enzyme preparation

Process Biochemistry - Tập 90 - Trang 66-80 - 2020
Min Sup Kim1, Roberto Fernández‐Lafuente2
1Laboratoire Réactions et Génie des Procédés
2Danmarks Tekniske Universitet = Technical University of Denmark

Tóm tắt

Từ khóa


Tài liệu tham khảo

Sheldon, 2012, Fundamentals of green chemistry: efficiency in reaction design (2012), Chem. Soc. Rev., 41, 1437, 10.1039/C1CS15219J

Pollard, 2007, Biocatalysis for pharmaceutical intermediates: the future is now, Trends Biotechnol., 25, 66, 10.1016/j.tibtech.2006.12.005

Woodley, 2008, New opportunities for biocatalysis: making pharmaceutical processes greener, Trends Biotechnol., 26, 321, 10.1016/j.tibtech.2008.03.004

Sheldon, 2018, Role of biocatalysis in sustainable chemistry, Chem. Rev., 118, 801, 10.1021/acs.chemrev.7b00203

Sheldon, 2019, Broadening the scope of biocatalysis in sustainable organic synthesis, ChemSusChem, 12, 2859, 10.1002/cssc.201900351

Thompson, 2019, Biocatalysis using immobilized enzymes in continuous flow for the synthesis of fine chemicals, Org. Process Res. Dev., 23, 9, 10.1021/acs.oprd.8b00305

Bezbradica, 2017, Enzymatic syntheses of esters - Green chemistry for valuable food, fuel and fine chemicals, Curr. Org. Chem., 21, 104, 10.2174/1385272821666161108123326

Schoemaker, 2003, Dispelling the myths - Biocatalysis in industrial synthesis, Science, 299, 1694, 10.1126/science.1079237

Serra, 2005, Biocatalytic preparation of natural flavours and fragrances, Trends Biotechnol., 23, 193, 10.1016/j.tibtech.2005.02.003

Aravindan, 2007, Lipase applications in food industry, Indian J. Biotechnol., 6, 141

Tan, 2010, Biodiesel production with immobilized lipase: a review, Biotechnol. Adv., 28, 628, 10.1016/j.biotechadv.2010.05.012

Gog, 2012, Biodiesel production using enzymatic transesterification - Current state and perspectives, Renew. Energy, 39, 10, 10.1016/j.renene.2011.08.007

Volpato, 2010, Use of enzymes in the production of semi-synthetic penicillins and cephalosporins: drawbacks and perspectives, Curr. Med. Chem., 17, 3855, 10.2174/092986710793205435

Fei, 2014, Bioconversion of natural gas to liquid fuel: opportunities and challenges, Biotechnol. Adv., 32, 596, 10.1016/j.biotechadv.2014.03.011

Sheldon, 2013, Enzyme immobilisation in biocatalysis: why, what and how, Chem. Soc. Rev., 42, 6223, 10.1039/C3CS60075K

Klibanov, 1989, Improving enzymes by using them in organic solvents, Nature, 409, 241, 10.1038/35051719

Dordick, 1989, Enzymatic catalysis in monophasic organic solvents, Enzyme Microb. Technol., 11, 194, 10.1016/0141-0229(89)90094-X

Klibanov, 1989, Enzymatic catalysis in anhydrous organic solvents, Trends Biochem. Sci., 14, 141, 10.1016/0968-0004(89)90146-1

Inada, 1986, Application of polyethylene glycol-modified enzymes in biotechnological processes: organic solvent-soluble enzymes, Trends Biotechnol., 4, 190, 10.1016/0167-7799(86)90244-1

Luisi, 1986, Solubilization of enzymes in apolar solvents via reverse micelles, Trends Biotechnol., 4, 153, 10.1016/0167-7799(86)90166-6

Ren, 2019, Recent progress in multienzymes co-immobilization and multienzyme system applications, Chem. Eng. J., 373, 1254, 10.1016/j.cej.2019.05.141

Barbosa, 2015, Strategies for the one-step immobilization-purification of enzymes as industrial biocatalysts, Biotechnol. Adv., 33, 435, 10.1016/j.biotechadv.2015.03.006

Bilal, 2019, Modifying bio-catalytic properties of enzymes for efficient biocatalysis: a review from immobilization strategies viewpoint, Biocatal. Biotransformation, 37, 159, 10.1080/10242422.2018.1564744

Hwang, 2019, Multienzymatic cascade reactions via enzyme complex by immobilization, ACS Catal., 9, 4402, 10.1021/acscatal.8b04921

Mateo, 2007, Improvement of enzyme activity, stability and selectivity via immobilization techniques, Enzyme Microb. Technol., 40, 1451, 10.1016/j.enzmictec.2007.01.018

Rodrigues, 2013, Modifying enzyme activity and selectivity by immobilization, Chem. Soc. Rev., 42, 6290, 10.1039/C2CS35231A

Garcia-Galan, 2011, Potential of different enzyme immobilization strategies to improve enzyme performance, Adv. Synth. Catal., 353, 2885, 10.1002/adsc.201100534

Santos, 2015, Importance of the support properties for immobilization or purification of enzymes, ChemCatChem, 7, 2413, 10.1002/cctc.201500310

Iyer, 2008, Enzyme stability and stabilization-Aqueous and non-aqueous environment, Process. Biochem., 43, 1019, 10.1016/j.procbio.2008.06.004

Brady, 2009, Advances in enzyme immobilisation, Biotechnol. Lett., 31, 1639, 10.1007/s10529-009-0076-4

Cao, 2005, Immobilized enzymes: Science or art?, Curr. Opin. Chem. Biol., 9, 217, 10.1016/j.cbpa.2005.02.014

Cao, 2003, Immobilised enzymes: Carrier-bound or carrier-free?, Curr. Opin. Biotechnol., 14, 387, 10.1016/S0958-1669(03)00096-X

Bilal, 2019, Modifying bio-catalytic properties of enzymes for efficient biocatalysis: a review from immobilization strategies viewpoint, Biocatalysis and Biotransformations, 37, 159, 10.1080/10242422.2018.1564744

Ren, 2019, Recent progress in multienzymes co-immobilization and multienzyme system applications, Chem. Eng. J., 373, 1254, 10.1016/j.cej.2019.05.141

Hwang, 2019, Multienzymatic cascade reactions via enzyme complex by immobilization, ACS Catal., 9, 4402, 10.1021/acscatal.8b04921

Bilal, 2019, Tailoring multipurpose biocatalysts via protein engineering approaches: a review, Catal. Letters, 149, 2204, 10.1007/s10562-019-02821-8

Shemsi, 2019, Site-directed chemically-modified magnetic enzymes: fabrication, improvements, biotechnological applications and future prospects, Biotechnol. Adv., 37, 357, 10.1016/j.biotechadv.2019.02.002

Bernal, 2018, Integrating enzyme immobilization and protein engineering: an alternative path for the development of novel and improved industrial biocatalysts, Biotechnol. Adv., 36, 1470, 10.1016/j.biotechadv.2018.06.002

Rodrigues, 2011, Coupling chemical modification and immobilization to improve the catalytic performance of enzymes, Adv. Synth. Catal., 353, 2216, 10.1002/adsc.201100163

Rodrigues, 2009, Immobilization-stabilization of the lipase from Thermomyces lanuginosus: critical role of chemical amination, Process. Biochem., 44, 963, 10.1016/j.procbio.2009.04.015

Rueda, 2016, Chemical modification in the design of immobilized enzyme biocatalysts: drawbacks and opportunities, Chem. Rec., 16, 1436, 10.1002/tcr.201600007

Rodrigues, 2014, Amination of enzymes to improve biocatalyst performance: coupling genetic modification and physicochemical tools, RSC Adv., 4, 38350, 10.1039/C4RA04625K

Cowan, 2011, Enhancing the functional properties of thermophilic enzymes by chemical modification and immobilization, Enzyme Microb. Technol., 49, 326, 10.1016/j.enzmictec.2011.06.023

Hernandez, 2011, Control of protein immobilization: coupling immobilization and site-directed mutagenesis to improve biocatalyst or biosensor performance, Enzyme Microb. Technol., 48, 107, 10.1016/j.enzmictec.2010.10.003

Barbosa, 2013, Heterofunctional supports in enzyme immobilization: from traditional immobilization protocols to opportunities in tuning enzyme properties, Biomacromolecules, 14, 2433, 10.1021/bm400762h

Virgen-Ortíz, 2016, Reuse of anion exchangers as supports for enzyme immobilization: reinforcement of the enzyme-support multiinteraction after enzyme inactivation, Process. Biochem., 51, 1391, 10.1016/j.procbio.2016.06.020

Barbosa, 2013, Heterofunctional supports in enzyme immobilization: from traditional immobilization protocols to opportunities in tuning enzyme properties, Biomacromolecules, 14, 2433, 10.1021/bm400762h

Virgen-Ortíz, 2017, Desorption of lipases immobilized on octyl-agarose beads and coated with ionic polymers after thermal inactivation. Stronger adsorption of polymers/unfolded protein composites, Molecules, 22, 10.3390/molecules22010091

Gonçalves, 2019, Trends on enzyme immobilization researches based on bibliometric analysis, Process. Biochem., 76, 95, 10.1016/j.procbio.2018.09.016

Kozuch, 2012, ‘Turning over’ definitions in catalytic cycles, ACS Catal., 2, 2787, 10.1021/cs3005264

Bligaard, 2016, Towards benchmarking in catalysis science: best practices, challenges and opportunities, ACS Catal., 6, 2590, 10.1021/acscatal.6b00183

Dias Gomes, 2019, Considerations when measuring biocatalyst performance, Molecules, 24, 10.3390/molecules24193573

Zucca, 2016, Agarose and its derivatives as supports for enzyme immobilization, Molecules, 21, 10.3390/molecules21111577

Mateo, 2005, Some special features of glyoxyl supports to immobilize proteins, Enzyme Microb. Technol., 37, 456, 10.1016/j.enzmictec.2005.03.020

Palomo, 2003, General trend of lipase to self-assemble giving bimolecular aggregates greatly modifies the enzyme functionality, Biomacromolecules, 4, 1, 10.1021/bm025729+

Wilson, 2006, Effect of lipase-lipase interactions in the activity, stability and specificity of a lipase from Alcaligenes sp, Enzyme Microb. Technol., 39, 259, 10.1016/j.enzmictec.2005.10.015

Fernández-Lorente, 2003, Self-assembly of Pseudomonas fluorescens lipase into bimolecular aggregates dramatically affects functional properties, Biotechnol. Bioeng., 82, 232, 10.1002/bit.10560

Palomo, 2004, Use of immobilized lipases for lipase purification via specific lipase-lipase interactions, Journal of Chromatography A, 1038, 267, 10.1016/j.chroma.2004.03.058

Palomo, 2005, Lipase-lipase interactions as a new tool to immobilize and modulate the lipase properties, Enzyme Microb. Technol., 36, 447, 10.1016/j.enzmictec.2004.09.013

Pessela, 2003, One-step purification, covalent immobilization, and additional stabilization of a thermophilic poly-his-tagged β-galactosidase from Thermus sp. Strain T2 by using novel heterofunctional chelate - Epoxy sepabeads, Biomacromolecules, 4, 107, 10.1021/bm020086j

Rocchietti, 2004, Immobilization and stabilization of recombinant multimeric uridine and purine nucleoside phosphorylases from Bacillus subtilis, Biomacromolecules, 5, 2195, 10.1021/bm049765f

Ubiali, 2004, Synthesis of 2′-deoxynucleosides by transglycosylation with new immobilized and stabilized uridine phosphorylase and purine nucleoside phosphorylase, Adv. Synth. Catal., 346, 1361, 10.1002/adsc.200404019

Bommarius, 2013, Stabilizing biocatalysts, Chem. Soc. Rev., 42, 6534, 10.1039/c3cs60137d

Mateo, 2006, Glyoxyl agarose: a fully inert and hydrophilic support for immobilization and high stabilization of proteins, Enzyme Microb. Technol., 39, 274, 10.1016/j.enzmictec.2005.10.014

Blanco, 1989, Stabilization of enzymes by multipoint covalent attachment to agarose-aldehyde gels. Borohydride reduction of trypsin-agarose derivatives, Enzyme Microb. Technol., 11, 360, 10.1016/0141-0229(89)90020-3

Guisán, 1988, Aldehyde-agarose gels as activated supports for immobilization-stabilization of enzymes, Enzyme Microb. Technol., 10, 375, 10.1016/0141-0229(88)90018-X

Orrego, 2018, Stabilization of enzymes by multipoint covalent attachment on aldehyde-supports: 2-picoline borane as an alternative reducing agent, Catalysts, 8, 10.3390/catal8080333

Barbosa, 2014, Glutaraldehyde in bio-catalysts design: a useful crosslinker and a versatile tool in enzyme immobilization, RSC Adv., 4, 1583, 10.1039/C3RA45991H

Virgen-Ortíz, 2017, Polyethylenimine: A very useful ionic polymer in the design of immobilized enzyme biocatalysts, J. Mater. Chem. B, 5, 7461, 10.1039/C7TB01639E

Katchalski-Katzir, 2000, A carrier for immobilization of enzymes of industrial potential, J. Mol. Catal. - B Enzym., 10, 157, 10.1016/S1381-1177(00)00124-7

Boller, 2002, EUPERGIT oxirane acrylic beads: how to make enzymes fit for biocatalysis, Org. Process Res. Dev., 6, 509, 10.1021/op015506w

Mateo, 2002, Epoxy Sepabeads: A novel epoxy support for stabilization of industrial enzymes via very intense multipoint covalent attachment, Biotechnol. Prog., 18, 629, 10.1021/bp010171n

Garcia-Galan, 2011, Potential of different enzyme immobilization strategies to improve enzyme performance, Adv. Synth. Catal., 353, 2885, 10.1002/adsc.201100534

Barbosa, 2013, Heterofunctional supports in enzyme immobilization: from traditional immobilization protocols to opportunities in tuning enzyme properties, Biomacromolecules, 14, 2433, 10.1021/bm400762h

Torres, 2003, A novel heterofunctional epoxy-amino sepabeads for a new enzyme immobilization protocol: immobilization-stabilization of β-galactosidase from Aspergillus oryzae, Biotechnol. Prog., 19, 1056, 10.1021/bp025771g

Rueda, 2015, Improved performance of lipases immobilized on heterofunctional octyl-glyoxyl agarose beads, RSC Adv., 5, 11212, 10.1039/C4RA13338B

Mateo, 2010, Improvement of enzyme properties with a two-step immobilizaton process on novel heterofunctional supports, Biomacromolecules, 11, 3112, 10.1021/bm100916r

Albuquerque, 2016, Easy stabilization of interfacially activated lipases using heterofunctional divinyl sulfone activated-octyl agarose beads. Modulation of the immobilized enzymes by altering their nanoenvironment, Process. Biochem., 51, 865, 10.1016/j.procbio.2016.04.002

Zaak, 2018, A new heterofunctional amino-vinyl sulfone support to immobilize enzymes: application to the stabilization of β-galactosidase from Aspergillus oryzae, Process. Biochem., 64, 200, 10.1016/j.procbio.2017.09.020

Barbosa, 2014, Glutaraldehyde in bio-catalysts design: a useful crosslinker and a versatile tool in enzyme immobilization, RSC Adv., 4, 1583, 10.1039/C3RA45991H

Betancor, 2006, Different mechanisms of protein immobilization on glutaraldehyde activated supports: effect of support activation and immobilization conditions, Enzyme Microb. Technol., 39, 877, 10.1016/j.enzmictec.2006.01.014

de Andrades, 2019, Immobilization and stabilization of different β-glucosidases using the glutaraldehyde chemistry: optimal protocol depends on the enzyme, Int. J. Biol. Macromol., 129, 672, 10.1016/j.ijbiomac.2019.02.057

Ait Braham, 2019, Cooperativity of covalent attachment and ion exchange on alcalase immobilization using glutaraldehyde chemistry: enzyme stabilization and improved proteolytic activity, Biotechnol. Prog., 35, 10.1002/btpr.2768

Siar, 2018, Immobilization/stabilization of ficin extract on glutaraldehyde-activated agarose beads. Variables that control the final stability and activity in protein hydrolyses, Catalysts, 8, 10.3390/catal8040149

Vazquez-Ortega, 2018, Stabilization of dimeric β-glucosidase from Aspergillus niger via glutaraldehyde immobilization under different conditions, Enzyme Microb. Technol., 110, 38, 10.1016/j.enzmictec.2017.12.007

Zaak, 2017, Exploiting the versatility of aminated supports activated with glutaraldehyde to immobilize β-galactosidase from Aspergillus oryzae, Catalysts, 7, 10.3390/catal7090250

Barbosa, 2012, Versatility of glutaraldehyde to immobilize lipases: effect of the immobilization protocol on the properties of lipase B from Candida antarctica, Process. Biochem., 47, 1220, 10.1016/j.procbio.2012.04.019

Rodrigues, 2019, Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions, Biotechnol. Adv., 37, 746, 10.1016/j.biotechadv.2019.04.003

Qin, 2019, One-step immobilization-purification of enzymes by carbohydrate-binding module family 56 tag fusion, Food Chem., 299, 10.1016/j.foodchem.2019.125037

Zhou, 2018, Facile oriented immobilization and purification of His-tagged organophosphohydrolase on viruslike mesoporous silica nanoparticles for organophosphate bioremediation, ACS Sustain. Chem. Eng., 6, 13588, 10.1021/acssuschemeng.8b04018

Zhou, 2017, Synchronized purification and immobilization of his-tagged β-glucosidase via Fe3O4/PMG core/shell magnetic nanoparticles, Sci. Rep., 7

Cao, 2017, Fabrication of Ni2+-nitrilotriacetic acid functionalized magnetic mesoporous silica nanoflowers for one pot purification and immobilization of His-tagged Ω-transaminase, Biochem. Eng. J., 128, 116, 10.1016/j.bej.2017.09.019

Döbber, 2016, New options for biocatalysis: merging purification and immobilization through innovative binding tags, Chemie-Ingenieur-Technik, 88, 1245, 10.1002/cite.201650087

Pessela, 2003, One-step purification, covalent immobilization, and additional stabilization of a thermophilic poly-his-tagged β-galactosidase from Thermus sp. strain T2 by using novel heterofunctional chelate - Epoxy sepabeads, Biomacromolecules, 4, 107, 10.1021/bm020086j

Mateo, 2001, One-step purification, covalent immobilization, and additional stabilization of poly-his-tagged proteins using novel heterofunctional chelate-epoxy supports, Biotechnol. Bioeng., 76, 269, 10.1002/bit.10019

Rodrigues, 2013, Modifying enzyme activity and selectivity by immobilization, Chem. Soc. Rev., 42, 6290, 10.1039/C2CS35231A

Hernandez, 2011, Control of protein immobilization: coupling immobilization and site-directed mutagenesis to improve biocatalyst or biosensor performance, Enzyme Microb. Technol., 48, 107, 10.1016/j.enzmictec.2010.10.003

Dal Magro, 2020, Pectin lyase immobilization using the glutaraldehyde chemistry increases the enzyme operation range, Enzyme Microb. Technol., 132, 10.1016/j.enzmictec.2019.109397

Dal Magro, 2019, Optimized immobilization of polygalacturonase from Aspergillus niger following different protocols: improved stability and activity under drastic conditions, Int. J. Biol. Macromol., 138, 234, 10.1016/j.ijbiomac.2019.07.092

Bilal, 2019, Engineering enzyme-coupled hybrid nanoflowers: the quest for optimum performance to meet biocatalytic challenges and opportunities, Int. J. Biol. Macromol., 135, 677, 10.1016/j.ijbiomac.2019.05.206

Bilal, 2019, Chemical, physical, and biological coordination: an interplay between materials and enzymes as potential platforms for immobilization, Coord. Chem. Rev., 388, 1, 10.1016/j.ccr.2019.02.024

Tran, 2018, Organic-inorganic hybrid nanoflowers as potent materials for biosensing and biocatalytic applications, Biochip J., 12, 268, 10.1007/s13206-018-2409-7

Celik, 2018, Formation of functional nanobiocatalysts with a novel and encouraging immobilization approach and their versatile bioanalytical applications, RSC Adv., 8, 25298, 10.1039/C8RA03250E

Altinkaynak, 2016, A new generation approach in enzyme immobilization: organic-inorganic hybrid nanoflowers with enhanced catalytic activity and stability, Enzyme Microb. Technol., 93–94, 105, 10.1016/j.enzmictec.2016.06.011

Wu, 2015, Metal-organic frameworks and inorganic nanoflowers: a type of emerging inorganic crystal nanocarrier for enzyme immobilization, Catal. Sci. Technol., 5, 5077, 10.1039/C5CY01181G

Lee, 2015, Organic-inorganic hybrid nanoflowers: types, characteristics, and future prospects, J. Nanobiotechnology, 13, 10.1186/s12951-015-0118-0

Rodrigues, 2019, Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions, Biotechnol. Adv., 37, 746, 10.1016/j.biotechadv.2019.04.003

Manoel, 2015, Immobilization of lipases on hydrophobic supports involves the open form of the enzyme, Enzyme Microb. Technol., 71, 53, 10.1016/j.enzmictec.2015.02.001

Zaak, 2018, A new heterofunctional amino-vinyl sulfone support to immobilize enzymes: application to the stabilization of β-galactosidase from Aspergillus oryzae, Process. Biochem., 64, 200, 10.1016/j.procbio.2017.09.020

Dos Santos, 2015, Bovine trypsin immobilization on agarose activated with divinylsulfone: improved activity and stability via multipoint covalent attachment, J. Mol. Catal., B Enzym., 117, 38, 10.1016/j.molcatb.2015.04.008

Vazquez-Ortega, 2018, Stabilization of dimeric β-glucosidase from Aspergillus niger via glutaraldehyde immobilization under different conditions, Enzyme Microb. Technol., 110, 38, 10.1016/j.enzmictec.2017.12.007

Siar, 2018, Immobilization/stabilization of ficin extract on glutaraldehyde-activated agarose beads. Variables that control the final stability and activity in protein hydrolyses, Catalysts, 8, 10.3390/catal8040149

Siar, 2017, Stabilization of ficin extract by immobilization on glyoxyl agarose. Preliminary characterization of the biocatalyst performance in hydrolysis of proteins, Process. Biochem., 58, 98, 10.1016/j.procbio.2017.04.009

Ranjbari, 2019, Improved features of a highly stable protease from Penaeus vannamei by immobilization on glutaraldehyde activated graphene oxide nanosheets, Int. J. Biol. Macromol., 130, 564, 10.1016/j.ijbiomac.2019.02.163

Pedroche, 2007, Effect of the support and experimental conditions in the intensity of the multipoint covalent attachment of proteins on glyoxyl-agarose supports: correlation between enzyme-support linkages and thermal stability, Enzyme Microb. Technol., 40, 1160, 10.1016/j.enzmictec.2006.08.023

Guisán, 1993, Stabilization of heterodimeric enzyme by multipoint covalent immobilization: penicillin G acylase from Kluyvera citrophila, Biotechnol. Bioeng., 42, 455, 10.1002/bit.260420408

Siar, 2019, Amination of ficin extract to improve its immobilization on glyoxyl-agarose: improved stability and activity versus casein, Int. J. Biol. Macromol., 133, 412, 10.1016/j.ijbiomac.2019.04.123

Tavano, 2018, Biotechnological applications of proteases in food technology, Compr. Rev. Food Sci. Food Saf., 17, 412, 10.1111/1541-4337.12326

Tardioli, 2003, Hydrolysis of proteins by immobilized-stabilized alcalase-glyoxyl agarose, Biotechnol. Prog., 19, 352, 10.1021/bp025588n

Tardioli, 2003, Design of new immobilized-stabilized carboxypeptidase a derivative for production of aromatic free hydrolysates of proteins, Biotechnol. Prog., 19, 565, 10.1021/bp0256364

Sousa, 2004, Kinetic model for whey protein hydrolysis by alcalase multipoint-immobilized on agarose gel particles, Braz. J. Chem. Eng., 21, 147, 10.1590/S0104-66322004000200003

Amaral-Fonseca, 2018, Preparation of magnetic cross-linked amyloglucosidase aggregates: solving some activity problems, Catalysts, 8, 10.3390/catal8110496

Pronk, 2014, Dynamic heterogeneity controls diffusion and viscosity near biological interfaces, Nat. Commun., 5, 3034, 10.1038/ncomms4034

Regan, 1974, Influence of intraparticle diffusional limitation on the observed kinetics of immobilized enzymes and on catalyst design, Biotechnol. Bioeng., 16, 1081, 10.1002/bit.260160808

Shen, 2007, Critical review of the impact of tortuosity on diffusion, Chem. Eng. Sci., 62, 3748, 10.1016/j.ces.2007.03.041

Bolivar, 2013, Shine a light on immobilized enzymes: real-time sensing in solid supported biocatalysts, Trends Biotechnol., 31, 194, 10.1016/j.tibtech.2013.01.004

Bolivar, 2016, Advanced characterization of immobilized enzymes as heterogeneous biocatalysts, Catal. Today, 80, 66, 10.1016/j.cattod.2015.05.004

Bhalerao, 2018, Ultrasound-assisted chemoenzymatic epoxidation of soybean oil by using lipase as biocatalyst, Ultrason. Sonochem., 40, 912, 10.1016/j.ultsonch.2017.08.042

Rokhina, 2009, Low-frequency ultrasound in biotechnology: state of the art, Trends Biotechnol., 27, 298, 10.1016/j.tibtech.2009.02.001

Veljković, 2012, Biodiesel production by ultrasound-assisted transesterification: state of the art and the perspectives, Renew. Sustain. Energy Rev., 16, 1193, 10.1016/j.rser.2011.11.022

Subhedar, 2013, Intensification of enzymatic hydrolysis of lignocellulose using ultrasound for efficient bioethanol production: a review, Ind. Eng. Chem. Res., 52, 11816, 10.1021/ie401286z

Martins, 2013, Ultrasound-assisted butyl acetate synthesis catalyzed by Novozym 435: enhanced activity and operational stability, Ultrason. Sonochem., 20, 1155, 10.1016/j.ultsonch.2013.01.018

Paludo, 2015, The combined use of ultrasound and molecular sieves improves the synthesis of ethyl butyrate catalyzed by immobilized Thermomyces lanuginosus lipase, Ultrason. Sonochem., 22, 89, 10.1016/j.ultsonch.2014.05.004

Patil, 2018, Ultrasound-assisted improvements in biocatalytic activity and production of organic-solvent stable protease from Bacillus circulans MTCC 7942, Ultrason. Sonochem., 40, 201, 10.1016/j.ultsonch.2017.07.012

Fernandez-Lopez, 2017, Effect of protein load on stability of immobilized enzymes, Enzyme Microb. Technol., 98, 18, 10.1016/j.enzmictec.2016.12.002

Zaak, 2017, Effect of immobilization rate and enzyme crowding on enzyme stability under different conditions. The case of lipase from Thermomyces lanuginosus immobilized on octyl agarose beads, Process. Biochem., 56, 117, 10.1016/j.procbio.2017.02.024

Mateo, 2006, Glyoxyl agarose: a fully inert and hydrophilic support for immobilization and high stabilization of proteins, Enzyme Microb. Technol., 39, 274, 10.1016/j.enzmictec.2005.10.014

Fernandez-Lafuente, 2009, Stabilization of multimeric enzymes: strategies to prevent subunit dissociation, Enzyme Microb. Technol., 45, 405, 10.1016/j.enzmictec.2009.08.009

Poltorak, 1998, Dissociative thermal inactivation, stability, and activity of oligomeric enzymes, Biochemistry (Moscow), 63, 303

Palomo, 2003, General trend of lipase to self-assemble giving bimolecular aggregates greatly modifies the enzyme functionality, Biomacromolecules, 4, 1, 10.1021/bm025729+

Wilson, 2006, Effect of lipase-lipase interactions in the activity, stability and specificity of a lipase from Alcaligenes sp, Enzyme Microb. Technol., 39, 259, 10.1016/j.enzmictec.2005.10.015

Fernández-Lorente, 2003, Self-assembly of Pseudomonas fluorescens lipase into bimolecular aggregates dramatically affects functional properties, Biotechnol. Bioeng., 82, 232, 10.1002/bit.10560

Palomo, 2004, Use of immobilized lipases for lipase purification via specific lipase-lipase interactions, J. Chromatogr. A, 1038, 267, 10.1016/j.chroma.2004.03.058

Palomo, 2005, Lipase-lipase interactions as a new tool to immobilize and modulate the lipase properties, Enzyme Microb. Technol., 36, 447, 10.1016/j.enzmictec.2004.09.013

Fernandez-Lorente, 2007, Improved catalytic properties of immobilized lipases by the presence of very low concentrations of detergents in the reaction medium, Biotechnol. Bioeng., 97, 242, 10.1002/bit.21230

Mogensen, 2005, Activation, inhibition, and destabilization of Thermomyces lanuginosus lipase by detergents, Biochemistry, 44, 1719, 10.1021/bi0479757

Barbosa, 2013, Heterofunctional supports in enzyme immobilization: from traditional immobilization protocols to opportunities in tuning enzyme properties, Biomacromolecules, 14, 2433, 10.1021/bm400762h

Dal Magro, 2020, Pectin lyase immobilization using the glutaraldehyde chemistry increases the enzyme operation range, Enzyme Microb. Technol., 132, 10.1016/j.enzmictec.2019.109397

Dal Magro, 2019, Optimized immobilization of polygalacturonase from Aspergillus niger following different protocols: improved stability and activity under drastic conditions, Int. J. Biol. Macromol., 138, 234, 10.1016/j.ijbiomac.2019.07.092

Virgen-Ortíz, 2017, Relevance of substrates and products on the desorption of lipases physically adsorbed on hydrophobic supports, Enzyme Microb. Technol., 96, 30, 10.1016/j.enzmictec.2016.09.010

Mateo, 2005, Some special features of glyoxyl supports to immobilize proteins, Enzyme Microb. Technol., 37, 456, 10.1016/j.enzmictec.2005.03.020

Fischer, 2010, Amine coupling through EDC/NHS: a practical approach, Methods Mol. Biol., 627, 55, 10.1007/978-1-60761-670-2_3

Jordan, 2011, Preparation and characterization of cellulase-bound magnetite nanoparticles, J. Mol. Catal., B Enzym., 68, 139, 10.1016/j.molcatb.2010.09.010

Sun, 2017, Stability and activity of immobilized trypsin on carboxymethyl chitosan-functionalized magnetic nanoparticles cross-linked with carbodiimide and glutaraldehyde, J. Chromatogr. B Analyt. Technol. Biomed. Life Sci., 1054, 57, 10.1016/j.jchromb.2017.04.016

Cao, 2000, Cross-linked enzyme aggregates: a simple and effective method for the immobilization of penicillin acylase, Org. Lett., 2, 1361, 10.1021/ol005593x

Sheldon, 2007, Cross-linked enzyme aggregates (CLEA®s): stable and recyclable biocatalysts, Biochem. Soc. Trans., 35, 1583, 10.1042/BST0351583

Sheldon, 2011, Cross-linked enzyme aggregates as industrial biocatalysts, Org. Process Res. Dev., 15, 213, 10.1021/op100289f

Šulek, 2011, Immobilization of horseradish peroxidase as crosslinked enzyme aggregates (CLEAs), Process. Biochem., 46, 765, 10.1016/j.procbio.2010.12.001

Wilson, 2006, CLEAs of lipases and poly-ionic polymers: a simple way of preparing stable biocatalysts with improved properties, Enzyme Microb. Technol., 39, 750, 10.1016/j.enzmictec.2005.12.011

Cruz, 2012, Optimized preparation of CALB-CLEAs by response surface methodology: the necessity to employ a feeder to have an effective crosslinking, J. Mol. Catal., B Enzym., 80, 7, 10.1016/j.molcatb.2012.04.013

Galvis, 2012, Chemical amination of lipase B from Candida antarctica is an efficient solution for the preparation of crosslinked enzyme aggregates, Process. Biochem., 47, 2373, 10.1016/j.procbio.2012.09.018

Amaral-Fonseca, 2018, Preparation of magnetic cross-linked amyloglucosidase aggregates: solving some activity problems, Catalysts, 8, 10.3390/catal8110496

Rojas, 2019, Preparation of crosslinked enzyme aggregates of a thermostable cyclodextrin glucosyltransferase from Thermoanaerobacter sp. Critical effect of the crosslinking agent, Catalysts, 9, 10.3390/catal9020120

Tükel, 2013, Preparation of crosslinked enzyme aggregates (CLEA) of catalase and its characterization, J. Mol. Catal., B Enzym., 97, 252, 10.1016/j.molcatb.2013.09.007

Sahutoglu, 2015, Immobilisation of Aspergillus oryzae α-amylase and Aspergillus niger glucoamylase enzymes as cross-linked enzyme aggregates, Chem. Pap., 69, 433, 10.1515/chempap-2015-0031

Zhang, 2016, Preparation of crosslinked enzyme aggregates (CLEAs) of acid urease with urethanase activity and their application, J. Basic Microbiol., 56, 422, 10.1002/jobm.201500498

Guimarães, 2018, Evaluation of strategies to produce highly porous cross-linked aggregates of porcine pancreas lipase with magnetic properties, Molecules, 23, 10.3390/molecules23112993

Tirunagari, 2018, Crosslinked enzyme aggregates (CLEA) of phytase with soymilk proteins, J. Biotechnol., 282, 67, 10.1016/j.jbiotec.2018.07.003

Rodrigues, 2019, Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions, Biotechnol. Adv., 37, 746, 10.1016/j.biotechadv.2019.04.003

Fernández-Lorente, 2005, Purification of different lipases from Aspergillus niger by using a highly selective adsorption on hydrophobic supports, Biotechnol. Bioeng., 92, 773, 10.1002/bit.20656

Palomo, 2002, Enzymatic production of (3S,4R)-(-)-4-(4′-fluorophenyl)-6-oxo-piperidin-3-carboxylic acid using a commercial preparation of lipase A from Candida antarctica: the role of a contaminant esterase, Tetrahedron Asymmetry, 13, 2653, 10.1016/S0957-4166(02)00754-1

Segura, 2004, Different properties of the lipases contained in porcine pancreatic lipase extracts as enantioselective biocatalysts, Biotechnol. Prog., 20, 825, 10.1021/bp034363p

Segura, 2006, Purification and identification of different lipases contained in PPL commercial extracts: a minor contaminant is the main responsible of most esterasic activity, Enzyme Microb. Technol., 39, 817, 10.1016/j.enzmictec.2006.01.007