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Immobilized Biocatalysts, 3rd Edition
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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 (28 February 2025) | Viewed by 3873

Special Issue Editors

Prof. Dr. Luciana R. B. Gonçalves

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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
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Nathália Saraiva Rios

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Guest Editor
Chemical Engineering Department, Federal University of Rio Grande do Norte, Natal, Brazil
Interests: Biocatalysis; enzyme immobilization; bioprocess
Special Issues, Collections and Topics in MDPI journals

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

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Catalysts is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2200 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

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

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Published Papers (2 papers)

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Research

24 pages, 5668 KiB  
Article
A New Multi-Active Heterogeneous Biocatalyst Prepared Through a Layer-by-Layer Co-Immobilization Strategy of Lipase and Laccase on Nanocellulose-Based Materials
by Kimberle Paiva dos Santos, Maíra Saldanha Duarte, Nathália Saraiva Rios, Ana Iraidy Santa Brígida and Luciana Rocha Barros Gonçalves
Catalysts 2025, 15(2), 99; https://doi.org/10.3390/catal15020099 - 21 Jan 2025
Viewed by 798
Abstract
Lipase from Pseudomonas fluorescens (PFL) and laccase from Trametes versicolor were co-immobilized onto nanocellulose (NC), using a layer-by-layer approach. Initially, PFL was adsorbed onto NC through ionic and hydrophobic interactions. To achieve higher PFL immobilization yield and activity, NC was functionalized with aldehyde [...] Read more.
Lipase from Pseudomonas fluorescens (PFL) and laccase from Trametes versicolor were co-immobilized onto nanocellulose (NC), using a layer-by-layer approach. Initially, PFL was adsorbed onto NC through ionic and hydrophobic interactions. To achieve higher PFL immobilization yield and activity, NC was functionalized with aldehyde groups through periodate oxidation (NCox) or glutaraldehyde activation (NC-GA). FTIR analysis confirmed these chemical modifications. Among the functionalized NCs, NCox showed the best capacity to retain higher amounts of PFL (maximum load: 20 mg/g), and this support was selected to proceed with the co-immobilization experiments. In this process, NCox-250-PFL (NCox activated with 250 µmol/g of aldehyde groups) was covered with polyethyleneimine (PEI), laccase was co-immobilized, and a crosslinking step using glutaraldehyde was used to covalently attach the enzymes to the support, producing the biocatalyst NCox-250-PFL-PEI-Lac-GA. Co-immobilized enzymes presented higher thermal stability (50 °C) than soluble enzymes; co-immobilized laccase retained 61.1% of its activity after 24 h, and PFL retained about 90% after 48 h of deactivation at 50 °C. In operational stability assays, the heterogeneous biocatalysts maintained more than 45% of their activity after five cycles of pNPB hydrolysis and ABTS oxidation. This co-immobilized biocatalyst, with its high stability and activity retention, is a promising multi-active heterogeneous biocatalyst for use in cascade reactions of industrial interest. Full article
(This article belongs to the Special Issue Immobilized Biocatalysts, 3rd Edition)
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14 pages, 2302 KiB  
Article
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; https://doi.org/10.3390/catal14020148 - 17 Feb 2024
Cited by 4 | Viewed by 2488
Abstract
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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