Is enzyme immobilization a mature discipline? Some critical considerations to capitalize on the benefits of immobilization
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 experi...
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Published in | Chemical Society reviews Vol. 51; no. 15; pp. 6251 - 629 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
London
Royal Society of Chemistry
01.08.2022
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Subjects | |
Online Access | Get full text |
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Summary: | 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.
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. |
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Bibliography: | Roberto Fernandez-Lafuente is a Research Professor at ICP-CSIC in Madrid, Spain. He has around 35 years' experience in studying the interactions between bio-macromolecules and supports, applying this to the preparation of biocatalysts and biosensors. His current research interests remain in enzyme immobilization, with particular focus on (1) enzyme co-immobilization, (2) effects of supports surface-enzyme on enzyme function, (3) enzyme stabilization, and (4) design of new immobilization/stabilization strategies. He has published over 500 scientific papers with an H index of 89 (Scopus). He has been recognized as highly cited researcher in the Clarivate lists of years 2019, 2020 and 2021. Dr Juan M. Bolivar is chemical engineer (2004, University of Granada) and PhD in sciences (2009, Complutense University of Madrid). He has been researcher at Institute of Catalysis (2005-2009, ICP-CSIC, Madrid), postdoc and and university assistant at the Graz University of Technology (Austria), 2010-2019. He is currently Senior Research Associate at the department of Chemical and Materials Engineering at the Complutense University of Madrid within excellence program "Atracción de Talento" from Madrid. Current interest lies in industrial biotechnology, design and characterization of heterogeneous biocatalysts catalysis, and bioprocess engineering in the context of integrated biorefineries and sustainable chemistry. John Woodley is a Professor at DTU Chemical Engineering in Denmark. He has around 35 years' experience in scaling-up and implementing new bioprocesses. His current research interests are in bioprocess science, with particular focus on (1) oxygen transfer, (2) selective separation, (3) enzyme stability, and (4) continuous processes. He has published around 300 scientific papers and 30 book chapters. In 2016, he was the elected Chair of the Biocatalysis GRC (USA) and in 2021 he was awarded an ERC Advanced Grant. He is a Fellow of the Institution of Chemical Engineers (UK) and a Fellow of the Royal Academy of Engineering (UK). ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 ObjectType-Review-3 content type line 23 |
ISSN: | 0306-0012 1460-4744 1460-4744 |
DOI: | 10.1039/d2cs00083k |