An overview of holocellulose-degrading enzyme immobilization for use in bioethanol production

Autor: Raissa Pieroni Vaz, Edivaldo Ximenes Ferreira Filho, Leonora Rios de Souza Moreira
Rok vydání: 2016
Předmět:
Zdroj: Journal of Molecular Catalysis B: Enzymatic. 133:127-135
ISSN: 1381-1177
Popis: Enzymes are biocatalysts with huge potential for industry because they have specific catalytic properties, are easy to produce, and are environmentally friendly. These biocatalysts are remarkable molecules for use in the field of bioprocessing technology. However, for certain biocatalytic processes, native enzymes do not meet the requirements for large-scale application; therefore, their natural properties need to be modulated. Another consideration is that the current global demands of the biotechnology industry require increasing productivity of processes and reduction of costs. In this context, enzyme immobilization can be a low-cost approach to the development of more robust and resistant systems to industrial conditions. Immobilized enzymes provide greater stability, sensitivity, and catalytic activity, than free enzymes do, in addition to improved purification processes and the potential for reuse of the enzymes. Among different classes of enzymes, holocellulases are important because they have a broad application spectrum in key industries, such as food, textiles, and biofuels, which are billion-dollar industries. We compiled recent reports of holocellulase immobilization achieved using different techniques, with the focus on the production of bioethanol, a product with growing global demand. In this review, we discuss the concept of immobilization, immobilization techniques, and the state of the art with respect to immobilized holocellulases. We also discuss recent trends in immobilization for second-generation ethanol production and future prospects for industrial applications of immobilized enzymes.
Databáze: OpenAIRE
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