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Catalysts
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Enzyme Catalysis and Enzyme Engineering
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Enzyme Catalysis and Enzyme Engineering

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

Deadline for manuscript submissions: closed (31 January 2025) | Viewed by 2290

Special Issue Editors

Prof. Dr. Lei Wang

E-Mail Website
Guest Editor
Key Laboratory of Molecular Enzymology and Engineering of Ministry of Education, Jilin University, Changchun 130023, China
Interests: biocatalysis; green synthesis; artificial metalloenzyme; immobilization; enzyme engineering
Dr. Fengxi Li

E-Mail Website
Guest Editor Assistant
Key Laboratory of Molecular Enzymology and Engineering of Ministry of Education, Jilin University, Changchun 130023, China
Interests: enzyme design; biocatalysis; enzyme engineering; chemoenzymatic synthesis; bio-organic chemistry

Special Issue Information

Dear Colleagues,

Enzyme catalysis offers several advantages over traditional organic reactions, particularly in terms of environmental impact, selectivity, and efficiency. By utilizing enzymes or whole cells as catalysts, biocatalysis makes it possible to carry out complex chemical transformations under mild conditions, reducing the need for harsh reaction conditions and generating less waste. Enzymes are highly specific catalysts that often catalyze reactions with excellent chemo-, regio-, and stereoselectivity. The application of enzyme catalysis in the synthesis of fine chemicals, such as pharmaceuticals, nutritional additives, and cosmetics, has been widespread. Many classic C–C and C–X bond formation reactions have been efficiently catalyzed by enzymes, enabling the production of complex molecules with high efficiency and selectivity. Immobilization allows the enzymes to be easily separated from the reaction mixture and reused, improving the overall process economics. Additionally, advancements in enzyme engineering and discovery have led to the development of new enzymes with enhanced properties, enabling precise transformations and molecular editing. Overall, the field of enzyme catalysis and enzyme engineering has experienced significant growth in recent years, driven by the increasing demand for sustainable and efficient synthetic methods. As researchers continue to explore and optimize enzymatic processes, we can expect further innovations and applications in various industries.

This Special Issue aims to collect recent advances in enzyme catalysis and enzyme engineering in various fields. We welcome original research, reviews, and perspectives, including but not limited to, the following scopes:

  • The application of enzymes in organic synthesis, especially enzyme biocatalytic promiscuity in enzymatic, non-natural reactions.
  • The regulation of the catalytic performance of enzymes, including immobilization, chemical modification, rational design, and directed evolution,
  • The development and applications of green reaction media for enzymatic reactions.
  • The development of enzymatic-chemical methods for green

If you would like to submit papers for publication in this Special Issue or have any questions, please contact the in-house Editor, Mr. Ives Liu (ives.liu@mdpi.com).

Prof. Dr. Lei Wang
Guest Editor

Dr. Fengxi Li
Guest Editor Assistant

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

  • biocatalysis
  • enzyme engineering
  • enzyme immobilization
  • biocatalytic promiscuity
  • non-natural reactions

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Further information on MDPI's Special Issue policies can be found here.

Published Papers (3 papers)

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Research

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13 pages, 2419 KiB  
Article
Enhancement of Enzyme Activity by Alternating Magnetic Field and Near-Infrared Irradiation
by Fang Wang, Yuchen Liu, Qikai Dong, Zihan Li, Senrong Liang, Tianyi Zhang, Liangtao Xu and Renjun Gao
Catalysts 2025, 15(4), 386; https://doi.org/10.3390/catal15040386 - 16 Apr 2025
Viewed by 215
Abstract
The enhancement of enzyme activity has garnered significant attention in biotransformation processes and applications. This enhancement is achieved through the use of specific nanomaterials (NMs) with unique physicochemical characteristics responsive to external stimuli. In this study, an enzyme–Fe3O4 nano-biocatalytic system [...] Read more.
The enhancement of enzyme activity has garnered significant attention in biotransformation processes and applications. This enhancement is achieved through the use of specific nanomaterials (NMs) with unique physicochemical characteristics responsive to external stimuli. In this study, an enzyme–Fe3O4 nano-biocatalytic system (NBS) was developed to enable real-time activation of enzymatic catalysis under alternating magnetic field (AMF) and near-infrared (NIR) irradiation using dual-functional Fe3O4 magnetic nanoparticles (MNPs). When exposed to an AMF, Fe3O4 MNPs generate molecular vibrations through mechanisms such as Néel or Brown relaxation while acting as a photothermal agent in response to NIR irradiation. The synergistic effect of AMF and NIR irradiation significantly enhanced energy transfer between the enzyme and Fe3O4 MNPs, resulting in a maximum 4.3-fold increase in enzyme activity. Furthermore, the system reduced aldol reaction time by 66% (from 4 h to 1.5 h) while achieving 90% product yield. Additionally, factors such as nanoparticle size and NIR power were found to play a critical role in the efficiency of this real-time regulation strategy. The results also demonstrate that the enzyme–Fe3O4 nanocomposites (NCs) significantly enhanced catalytic efficiency and reduced the reaction time for aldol reactions. This study demonstrates an efficient NBS controlled via the synergistic effects of AMF and NIR irradiation, enabling spatiotemporal control of biochemical reactions. This work also provides a breakthrough strategy for dynamic biocatalysis, with potential applications in industrial biomanufacturing, on-demand drug synthesis, and precision nanomedicine. Full article
(This article belongs to the Special Issue Enzyme Catalysis and Enzyme Engineering)
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14 pages, 3915 KiB  
Article
Immobilization of Laccase in β-Cyclodextrin Composite Hydrogel for Efficient Degradation of Dye Pollutants
by Hong Zhang, Zhi Wang, Fengxi Li, Lei Wang and Bo Ren
Catalysts 2024, 14(8), 473; https://doi.org/10.3390/catal14080473 - 24 Jul 2024
Viewed by 1195
Abstract
A stable and efficient biocatalyst was prepared by encapsulating Trametes versicolor laccase using an acrylic acid-grafted β-cyclodextrin hydrogel (Lac-CD-PAA). Scanning electron microscopy and nitrogen adsorption-desorption experiments showed that there were regularly distributed channels in the spongy Lac-CD-PAA. In addition, a large number of [...] Read more.
A stable and efficient biocatalyst was prepared by encapsulating Trametes versicolor laccase using an acrylic acid-grafted β-cyclodextrin hydrogel (Lac-CD-PAA). Scanning electron microscopy and nitrogen adsorption-desorption experiments showed that there were regularly distributed channels in the spongy Lac-CD-PAA. In addition, a large number of mesopores and macropores existed in the wall of the hydrogel lamellae. This network structure reduced the diffusion resistance of the hydrogel to the target substrate. The relative activity of the resulting Lac-CD-PAA could be maintained at 35.8% after six cycles of use. Lac-CD-PAA exhibited higher thermal and chemical stability compared to free laccase. The negative charge on the surface of Lac-CD-PAA gives it the ability to pretreat cationic dyes. In six consecutive methylene blue decolorization tests, Lac-CD-PAA decolorized better than free laccase. The results showed that the prepared β-cyclodextrin-based composite hydrogel was a good carrier for laccase. Full article
(This article belongs to the Special Issue Enzyme Catalysis and Enzyme Engineering)
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Review

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17 pages, 8345 KiB  
Review
Harnessing Alcohol Dehydrogenases in Organic Reaction Cascades: A Strategy for Enhanced Efficiency in Synthetic Organic Chemistry
by Heba Abuzenah, Muhammad Abdulrasheed, Auwal Eshi Sardauna, Bayan Al-Qataisheh and Musa M. Musa
Catalysts 2025, 15(3), 223; https://doi.org/10.3390/catal15030223 - 27 Feb 2025
Viewed by 535
Abstract
Alcohol dehydrogenases (ADHs) are versatile enzymes that enable the reversible reduction of aldehydes and ketones to their corresponding alcohols. The exceptional chemo-, regio-, and stereoselectivity of ADHs position them as attractive catalysts for generating enantiopure alcohols, whether through deracemization of racemates or asymmetric [...] Read more.
Alcohol dehydrogenases (ADHs) are versatile enzymes that enable the reversible reduction of aldehydes and ketones to their corresponding alcohols. The exceptional chemo-, regio-, and stereoselectivity of ADHs position them as attractive catalysts for generating enantiopure alcohols, whether through deracemization of racemates or asymmetric reduction of prochiral ketones. The emergence of robust ADHs capable of functioning effectively at elevated temperatures and in high concentrations of non-aqueous media has stimulated interest in integrating ADH-catalyzed asymmetric transformations with other chemical processes in a single pot, either in a stepwise mode or simultaneously. This review presents an overview of one-pot organic transformations that combine ADH-catalyzed asymmetric reductions with additional nonenzymatic chemical reactions, demonstrating the potential for enhanced efficiency and sustainability in synthetic organic chemistry. Full article
(This article belongs to the Special Issue Enzyme Catalysis and Enzyme Engineering)
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