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      Is enzyme immobilization a mature discipline? Some critical considerations to capitalize on the benefits of immobilization

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          Abstract

          Enzyme immobilization has been developing since the 1960s and although many industrial biocatalytic processes use the technology to improve enzyme performance, still today we are far from full exploitation of the field.

          Abstract

          Enzyme immobilization has been developing since the 1960s and although many industrial biocatalytic processes use the technology to improve enzyme performance, still today we are far from full exploitation of the field. One clear reason is that many evaluate immobilization based on only a few experiments that are not always well-designed. In contrast to many other reviews on the subject, here we highlight the pitfalls of using incorrectly designed immobilization protocols and explain why in many cases sub-optimal results are obtained. We also describe solutions to overcome these challenges and come to the conclusion that recent developments in material science, bioprocess engineering and protein science continue to open new opportunities for the future. In this way, enzyme immobilization, far from being a mature discipline, remains as a subject of high interest and where intense research is still necessary to take full advantage of the possibilities.

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          Most cited references508

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          Metal-organic frameworks: opportunities for catalysis.

          The role of metal-organic frameworks (MOFs) in the field of catalysis is discussed, and special focus is placed on their assets and limits in light of current challenges in catalysis and green chemistry. Their structural and dynamic features are presented in terms of catalytic functions along with how MOFs can be designed to bridge the gap between zeolites and enzymes. The contributions of MOFs to the field of catalysis are comprehensively reviewed and a list of catalytic candidates is given. The subject is presented from a multidisciplinary point of view covering solid-state chemistry, materials science, and catalysis.
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            Nanocellulose in biomedicine: Current status and future prospect

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              Modifying enzyme activity and selectivity by immobilization.

              Immobilization of enzymes may produce alterations in their observed activity, specificity or selectivity. Although in many cases an impoverishment of the enzyme properties is observed upon immobilization (caused by the distortion of the enzyme due to the interaction with the support) in some instances such properties may be enhanced by this immobilization. These alterations in enzyme properties are sometimes associated with changes in the enzyme structure. Occasionally, these variations will be positive. For example, they may be related to the stabilization of a hyperactivated form of the enzyme, like in the case of lipases immobilized on hydrophobic supports via interfacial activation. In some other instances, these improvements will be just a consequence of random modifications in the enzyme properties that in some reactions will be positive while in others may be negative. For this reason, the preparation of a library of biocatalysts as broad as possible may be a key turning point to find an immobilized biocatalyst with improved properties when compared to the free enzyme. Immobilized enzymes will be dispersed on the support surface and aggregation will no longer be possible, while the free enzyme may suffer aggregation, which greatly decreases enzyme activity. Moreover, enzyme rigidification may lead to preservation of the enzyme properties under drastic conditions in which the enzyme tends to become distorted thus decreasing its activity. Furthermore, immobilization of enzymes on a support, mainly on a porous support, may in many cases also have a positive impact on the observed enzyme behavior, not really related to structural changes. For example, the promotion of diffusional problems (e.g., pH gradients, substrate or product gradients), partition (towards or away from the enzyme environment, for substrate or products), or the blocking of some areas (e.g., reducing inhibitions) may greatly improve enzyme performance. Thus, in this tutorial review, we will try to list and explain some of the main reasons that may produce an improvement in enzyme activity, specificity or selectivity, either real or apparent, due to immobilization.

                Author and article information

                Contributors
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                Journal
                CSRVBR
                Chemical Society Reviews
                Chem. Soc. Rev.
                Royal Society of Chemistry (RSC)
                0306-0012
                1460-4744
                August 01 2022
                2022
                : 51
                : 15
                : 6251-6290
                Affiliations
                [1 ]FQPIMA group, Chemical and Materials Engineering Department, Faculty of Chemical Sciences, Complutense University of Madrid, Madrid, 28040, Spain
                [2 ]Department of Chemical and Biochemical Engineering, Technical University of Denmark, 2800 Kgs Lyngby, Denmark
                [3 ]Departamento de Biocatálisis. ICP-CSIC, C/Marie Curie 2, Campus UAM-CSIC Cantoblanco, Madrid 28049, Spain
                [4 ]Center of Excellence in Bionanoscience Research, External Scientific Advisory Academic, King Abdulaziz University, Jeddah 21589, Saudi Arabia
                Article
                10.1039/D2CS00083K
                35838107
                5f269023-fe9a-4c60-8dd0-56402da90c71
                © 2022

                http://creativecommons.org/licenses/by-nc/3.0/

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