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Potential of Different Enzyme Immobilization Strategies to Improve Enzyme Performance

Garcia-Galan, Cristina ; Berenguer-Murcia, Ángel ; Fernandez-Lafuente, Roberto ; Rodrigues, Rafael C.

Advanced synthesis & catalysis, 2011-11, Vol.353 (16), p.2885-2904 [Periódico revisado por pares]

Weinheim: WILEY-VCH Verlag

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  • Título:
    Potential of Different Enzyme Immobilization Strategies to Improve Enzyme Performance
  • Autor: Garcia-Galan, Cristina ; Berenguer-Murcia, Ángel ; Fernandez-Lafuente, Roberto ; Rodrigues, Rafael C.
  • Assuntos: Analytical, structural and metabolic biochemistry ; Bioconversions. Hemisynthesis ; Biological and medical sciences ; Biotechnology ; biotransformations ; enzyme catalysis ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Immobilization ; Methods. Procedures. Technologies ; Nanoparticles ; nanotechnology ; Optimization ; Performance enhancement ; protein engineering ; protein modifications ; Proteins ; Reusable ; Stability ; Strategy
  • É parte de: Advanced synthesis & catalysis, 2011-11, Vol.353 (16), p.2885-2904
  • Notas: ArticleID:ADSC201100534
    istex:C9E885099DF1C11943E146205D0DDC8682047A2D
    ark:/67375/WNG-RP4KCMW7-K
    Spanish Ministerio de Ciencia e Innovación - No. CTQ2009-07568
    Spanish Ministerio de Ciencia e Innovación - No. Ramon y Cajal fellowship (RyC-2009-03813)
    Spanish Ministerio de Ciencia e Innovación - No. FPI predoctoral fellowship
    ObjectType-Article-1
    SourceType-Scholarly Journals-1
    ObjectType-Feature-2
    content type line 23
  • Descrição: 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).
  • Editor: Weinheim: WILEY-VCH Verlag
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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