Immobilized Biocatalysts, 3rd Edition

A special issue of Catalysts (ISSN 2073-4344). This special issue belongs to the section "Biocatalysis".

Deadline for manuscript submissions: closed (15 May 2024) | Viewed by 1500

Special Issue Editors

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Guest Editor
Departamento de Engenharia Química, Universidade Federal do Ceará, Campus do Pici, Bloco 709, CEP 60455760, Fortaleza 60000-000, CE, Brazil
Interests: biocatalysis; enzyme immobilization; bioprocess engineering and biochemical reaction engineering
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Guest Editor
Department of Chemical Engineering, Campus Central, Federal University of Rio Grande do Norte, Natal 59078-970, RN, Brazil
Interests: enzyme immobilization; biocatalysis; lipases; cellulase

Special Issue Information

Dear Colleagues,

This Special Issue is a continuation of the previous successful Special Issues “Immobilized Biocatalysts” and “Immobilized Biocatalysts II”.

Although enzymes as catalysts are environmentally beneficial, their applications require a certain degree of profitability to justify their cost competitiveness with conventional chemical catalysts. To make enzymatic biocatalysts increasingly economically viable, advances in modern biotechnology and protein engineering have contributed to improving various production processes. However, because the implementation of bioprocesses is a reality in industry, some critical obstacles still need to be overcome. For example, the efficiency of enzymatic processes can be increased by using immobilized catalysts (heterogeneous biocatalysts). In this way, it is possible to protect enzymes from various interactions with a reaction medium, increase their stability, allow reuse, or prolong a bioreactor’s operation time. Immobilization also increases the shelf life of an enzyme, thus facilitating its large-scale use and the economic formulation of biotechnological industries. There are several ways to immobilize enzymes, and three of the most common methods are physical adsorption, cross-linking or covalent bonding, and encapsulation. However, despite the great diversity of methods developed to date, no general approach applies to all enzymes. Therefore, for each case (process) it is necessary to choose the most straightforward and cheapest protocol that will result in a biocatalyst with high operational activity as well as stability. In this context, this Special Issue aims to bring together contributions for improving immobilized enzyme performance. The idea is not limited to biocatalyst preparation; the study of kinetics and reactor design is also welcome, including mass transfer limitations and scale-up.

Prof. Dr. Luciana R. B. Gonçalves
Prof. Dr. Nathália Saraiva Rios
Guest Editors

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  • enzyme immobilization
  • heterogeneous biocatalysts
  • enzyme stabilization
  • novel immobilization platforms
  • bioreactor design

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Published Papers (1 paper)

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14 pages, 2302 KiB  
Immobilization of Alcohol Dehydrogenases on Silica-Based Supports and Their Application in Enantioselective Ketone Reductions
by Daria Armani, Oreste Piccolo and Antonella Petri
Catalysts 2024, 14(2), 148; - 17 Feb 2024
Viewed by 1240
The use of immobilized alcohol dehydrogenases (ADHs) offers numerous advantages, especially in the reaction conditions required by industrial applications. Looking for more efficient and cost-effective methods of ADH immobilization, in this study we explored silica-based supports as an alternative to the use of [...] Read more.
The use of immobilized alcohol dehydrogenases (ADHs) offers numerous advantages, especially in the reaction conditions required by industrial applications. Looking for more efficient and cost-effective methods of ADH immobilization, in this study we explored silica-based supports as an alternative to the use of functionalized polymeric resins. Three commercially available ADHs were immobilized by adsorption and covalent bond formation. The obtained supported biocatalysts were applied for the bioreduction of acetophenone and some derivatives with good yields and excellent enantioselectivity. The important intermediate (S)-1-[3,5-bis(trifluoromethyl)phenyl]ethanol was obtained with a high enantiomeric excess (>99%) by using the highest performing immobilized ADH sample. The reusability of this biocatalyst was investigated in a flow system for five consecutive runs; the experiments showed that the biocatalyst could be recycled without a loss of activity and enantioselectivity. Finally, cross-linking with the glutaraldehyde of the supported biocatalyst was also carried out to prevent the leaching of the enzyme during the catalytic reactions. Full article
(This article belongs to the Special Issue Immobilized Biocatalysts, 3rd Edition)
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