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Potential Of Different Enzyme Immobilization Strategies To Improve Enzyme Performance

Cristina Garcia-Galan, Angel Berenguer-Murcia, Roberto Fernandez-Lafuente, Rafael C. Rodrigues
Published 2011 · Chemistry
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Enzyme biocatalysis plays a very relevant role in the development of many chemical industries, e.g., energy, food or fine chemistry. To achieve this goal, enzyme immobilization is a usual pre-requisite as a solution to get reusable biocatalysts and thus decrease the price of this relatively expensive compound. However, a proper immobilization technique may permit far more than to get a reusable enzyme; it may be used to improve enzyme performance by improving some enzyme limitations: enzyme purity, stability (including the possibility of enzyme reactivation), activity, specificity, selectivity, or inhibitions. Among the diverse immobilization techniques, the use of pre-existing supports to immobilize enzymes (via covalent or physical coupling) and the immobilization without supports [enzyme crosslinked aggregates (CLEAs) or crystals (CLECs)] are the most used or promising ones. This paper intends to give the advantages and disadvantages of the different existing immobilization strategies to solve the different aforementioned enzyme limitations. Moreover, the use of nanoparticles as immobilization supports is achieving an increasing importance, as the nanoparticles versatility increases and becomes more accessible to the researchers. We will also discuss here some of the advantages and drawbacks of these non porous supports compared to conventional porous supports. Although there are no universal optimal solutions for all cases, we will try to give some advice to select the optimal strategy for each particular enzyme and process, considering the enzyme properties, nature of the process and of the substrate. In some occasions the selection will be compulsory, for example due to the nature of the substrate. In other cases the optimal biocatalyst may depend on the company requirements (e.g., volumetric activity, enzyme stability, etc).



This paper is referenced by
10.1016/j.ijbiomac.2018.07.187
Enhancement of catalytic performance of porcine pancreatic lipase immobilized on functional ionic liquid modified Fe3O4-Chitosan nanocomposites.
Hongbo Suo (2018)
10.1080/10242422.2019.1602610
Fine-tuned preparation of cross-linked laccase nanoaggregates
Arif Sercan Şahutoğlu (2019)
10.3390/molecules190812461
Trends in Protein-Based Biosensor Assemblies for Drug Screening and Pharmaceutical Kinetic Studies
Ana Mafalda Gonçalves (2014)
10.3390/molecules22122165
Synthesis of Benzyl Acetate Catalyzed by Lipase Immobilized in Nontoxic Chitosan-Polyphosphate Beads
Ana Duarte Melo (2017)
10.7852/ijie.2013.27.2.322
Operation Modes Can Affect the Activity of Immobilized Enzyme onto Silk Fibroin Nanofibrous Membrane
Hanjin Oh (2013)
10.18593/eba.v19i2.20116
Esterification of acetic acid with alcohol isoamyl in the presence of enzymatic catalyst
N. L. D. Nyari (2019)
10.3390/molecules25051067
Free and Immobilized Lecitase™ Ultra as the Biocatalyst in the Kinetic Resolution of (E)-4-Arylbut-3-en-2-yl Esters
Aleksandra Leśniarek (2020)
10.3390/CATAL9070576
Increasing the enzyme loading capacity of porous supports by a layer-by-layer immobilization strategy using PEI as glue
Nathalia Saraiva Rios (2019)
10.1016/j.colsurfb.2019.03.071
Encapsulated functionalized stereocomplex PLA particles: An effective system to support mucolytic enzymes.
Stefania Boi (2019)
10.1111/JFBC.12564
β‐galactosidase: Biotechnological applications in food processing
Janifer Raj Xavier (2018)
10.1016/J.REACTFUNCTPOLYM.2018.12.013
Chitosan Co-polymeric nanostructures for catalase immobilization
Tülden Inanan (2019)
10.1016/J.BEJ.2019.03.002
Meso-molding three-dimensionally ordered macroporous alumina: A new platform to immobilize enzymes with high performance
Liya Zhou (2019)
10.1080/10242422.2018.1530766
Improvement of activity and stability of Rhizomucor miehei lipase by immobilization on nanoporous aluminium oxide and potassium sulfate microcrystals and their applications in the synthesis of aroma esters
Deniz Yıldırım (2019)
10.3390/CATAL8080333
Stabilization of Enzymes by Multipoint Covalent Attachment on Aldehyde-Supports: 2-Picoline Borane as an Alternative Reducing Agent
Alejandro H. Orrego (2018)
10.3390/CATAL8040170
Maltose Production Using Starch from Cassava Bagasse Catalyzed by Cross-Linked β-Amylase Aggregates
R. A. de Araujo-Silva (2018)
10.3390/molecules21111577
Agarose and Its Derivatives as Supports for Enzyme Immobilization
Paolo Zucca (2016)
10.2174/2213529404666180222114609
Immobilization of Cholesterol Oxidase: An Overview
Shubhrima Ghosh (2018)
10.3390/bios2010101
Enzyme-Gelatin Electrochemical Biosensors: Scaling Down
Karolien De Wael (2012)
10.1007/s12010-018-2927-8
Enhanced Properties and Lactose Hydrolysis Efficiencies of Food-Grade β-Galactosidases Immobilized on Various Supports: a Comparative Approach
Priti Katrolia (2018)
10.3390/molecules24193460
The Microenvironment in Immobilized Enzymes: Methods of Characterization and Its Role in Determining Enzyme Performance
Juan M Bolivar (2019)
10.1016/j.reactfunctpolym.2019.104454
Epoxy functionalized polymer grafted magnetic nanoparticles by facile surface initiated polymerization for immobilization studies of Candida Antarctica lipase B
Haq Asif Afzal (2020)
10.1016/J.PROCBIO.2019.07.001
Tuning dimeric formate dehydrogenases reduction/oxidation activities by immobilization
Deniz Yıldırım (2019)
10.1016/j.lwt.2020.109460
Co-immobilization of β-fructofuranosidase and glucose oxidase improves the stability of Bi-enzymes and the production of lactosucrose
Jie Long (2020)
10.1016/J.PROCBIO.2018.08.017
Efficient carbon dioxide sequestration by using recombinant carbonic anhydrase
Shih I. Tan (2018)
10.3390/molecules21050646
Reversible Immobilization of Lipases on Heterofunctional Octyl-Amino Agarose Beads Prevents Enzyme Desorption
Nazzoly Rueda (2016)
10.1080/10242422.2018.1458842
Improving reuse cycles of Thermomyces lanuginosus lipase (NS-40116) by immobilization in flexible polyurethane
Bruno R. Facin (2018)
10.1016/j.ijbiomac.2017.03.119
Expression of chitinase gene in BL21 pET system and investigating the biocatalystic performance of chitinase-loaded AlgSep nanocomposite beads.
Reza Mohammadzadeh (2017)
10.1016/j.enzmictec.2017.07.008
Preparation, activity and structure of cross-linked enzyme aggregates (CLEAs) with nanoparticle.
Shu-guang Wang (2017)
10.3390/molecules21081074
Immobilization of Glycoside Hydrolase Families GH1, GH13, and GH70: State of the Art and Perspectives
Natália Guilherme Graebin (2016)
10.1002/bit.24873
Quantitating intraparticle O2 gradients in solid supported enzyme immobilizates: experimental determination of their role in limiting the catalytic effectiveness of immobilized glucose oxidase.
Juan M Bolivar (2013)
10.2174/138527212804004526
Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison
Karel Morlans Hernández (2012)
10.1007/s10311-019-00942-5
Chitin and chitosan-based support materials for enzyme immobilization and biotechnological applications
Madan L. Verma (2019)
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