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Potential of Different Enzyme Immobilization Strategies to Improve Enzyme Performance by Cristina Garcia‐Galan; Ángel Berenguer‐Murcia; Roberto Fernandez‐Lafuente; Rafael C. Rodrigues is a Chemistry article available to read on EtoBox.
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## Abstract 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 versa
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- Author
- Cristina Garcia‐Galan; Ángel Berenguer‐Murcia; Roberto Fernandez‐Lafuente; Rafael C. Rodrigues
- Publisher
- John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Ltd.; Wiley - V C H Verlag GmbbH & Co.; Wiley (ISSN 1615-4150)
- Published
- 2011
- Language
- EN
- Field
- Chemistry (Physical Sciences)