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Modern Trends of Biocatalysis in Organic Chemistry and Enzyme Engineering–2nd Edition

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Bioorganic Chemistry".

Deadline for manuscript submissions: 31 December 2024 | Viewed by 2653

Special Issue Editors

College of Chemical and Biological Engineering, Zhejiang University, Hangzhou 310027, China
Interests: biocatalysis; biotrans; chiral synthesis; enzymatic-cat; chemo-enzymatic cat
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Guest Editor
State Key Laboratory of Materials-Oriented Chemical Engineering, School of Pharmaceutical Sciences, Nanjing Tech University, Nanjing 210009, China
Interests: industrial biocatalysis; green organic synthesis; enzyme engineering; synergistic catalysis of metal-enzyme
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

With the depletion of non-renewable resources and the proliferation of environmental pollution, organic reactions, which consume a significant quantity of organic solvents, are considered to be environmentally unfriendly. As a practical and sustainable alternative to traditional organic reactions, biocatalysis exhibits its substantial advantages in selectivity and efficiency. Many classic C–C and C–X bond formation reactions can be efficiently catalyzed by biocatalysts, and have been widely employed in the synthesis of fine chemicals such as pharmaceuticals and their intermediates, nutritional additives, cosmetics, etc. Various solvents have been developed and applied as the media for enzymatic reactions, and various immobilization materials and methods have been created to enhance the stability of enzymes. Moreover, the increasing demand for efficient and versatile synthetic methods, combined with powerful new discoveries and engineering tools, have prompted innovations in biocatalysis, particularly the development of novel enzymes for precise transformations or “molecular editing”. As a result, the past decade has witnessed an impressive expansion of biocatalysis.

This Special Issue, entitled “Modern Trends of Biocatalysis in Organic Chemistry and Enzyme Engineering”, aims to offer an open forum in which researchers may share their achievements regarding enzyme engineering and its applications in organic synthesis. Contributions to this Special Issue, in the form of both original research and review articles, may cover the enhancement of the catalytic performance of enzymes (including immobilization, chemical modification, rational design and directed evolution), the application of biocatalysts in organic synthesis, biocatalytic promiscuity, the development and utilization of green solvents for enzymatic reactions, enzymatic–chemical methods for the synthesis of fine chemicals, multi-enzyme synergistic catalysis, photo–enzyme synergistic catalysis, and others.

Dr. Gang Xu
Prof. Dr. Yi Hu
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. Molecules is an international peer-reviewed open access semimonthly 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 2700 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 engineering
  • biocatalytic promiscuity
  • enzyme immobilization
  • directed evolution
  • biocatalysis
  • enzymatic reactions

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Published Papers (4 papers)

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Research

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16 pages, 5642 KiB  
Article
Functionalized Ionic Liquids-Modified Metal–Organic Framework Material Boosted the Enzymatic Performance of Lipase
by Liran Ji, Wei Zhang, Yifei Zhang, Binbin Nian and Yi Hu
Molecules 2024, 29(10), 2381; https://doi.org/10.3390/molecules29102381 - 18 May 2024
Viewed by 427
Abstract
The development of immobilized enzymes with high activity and stability is critical. Metal–organic frameworks (MOFs) have attracted much academic and industrial interest in the field of enzyme immobilization due to their unique properties. In this study, the amino-functionalized ionic liquid (NIL)-modified metal–organic framework [...] Read more.
The development of immobilized enzymes with high activity and stability is critical. Metal–organic frameworks (MOFs) have attracted much academic and industrial interest in the field of enzyme immobilization due to their unique properties. In this study, the amino-functionalized ionic liquid (NIL)-modified metal–organic framework (UiO-66-NH2) was prepared to immobilize Candida rugosa lipase (CRL), using dialdehyde starch (DAS) as the cross-linker. The results of the Fourier transform infrared (FT-IR) spectra, X-ray powder diffraction (XRD), and scanning electronic microscopy (SEM) confirmed that the NIL was successfully grafted to UiO-66-NH2. The CRL immobilized on NIL-modified UiO-66-NH2 (UiO-66-NH2-NIL-DAS@CRL) exhibited satisfactory activity recovery (79.33%), stability, reusability, and excellent organic solvent tolerance. The research results indicated that ionic liquid-modified UiO-66-NH2 had practical potential for application in enzyme immobilization. Full article
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13 pages, 2833 KiB  
Article
A Simple Screening and Optimization Bioprocess for Long-Chain Peptide Catalysts Applied to Asymmetric Aldol Reaction
by Shulin Wang, Haidong Teng, Lan Wang, Pengcheng Li, Xinghao Yuan, Xi Sang, Jianping Wu, Lirong Yang and Gang Xu
Molecules 2023, 28(19), 6985; https://doi.org/10.3390/molecules28196985 - 9 Oct 2023
Viewed by 993
Abstract
Peptides have demonstrated their efficacy as catalysts in asymmetric aldol reactions. But the constraints inherent in chemical synthesis have imposed limitations on the viability of long-chain peptide catalysts. A noticeable dearth of tools has impeded the swift and effective screening of peptide catalysts [...] Read more.
Peptides have demonstrated their efficacy as catalysts in asymmetric aldol reactions. But the constraints inherent in chemical synthesis have imposed limitations on the viability of long-chain peptide catalysts. A noticeable dearth of tools has impeded the swift and effective screening of peptide catalysts using biological methods. To address this, we introduce a straightforward bioprocess for the screening of peptide catalysts for asymmetric aldol reactions. We synthesized several peptides through this method and obtained a 15-amino acid peptide. This peptide exhibited asymmetric aldol catalytic activity, achieving 77% ee in DMSO solvent and 63% ee with over an 80.8% yield in DMSO mixed with a pH 9.0 buffer solution. The successful application of our innovative approach not only represents an advancement but also paves the way for currently unexplored research avenues. Full article
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Review

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23 pages, 2093 KiB  
Review
Solvent Tolerance Improvement of Lipases Enhanced Their Applications: State of the Art
by Mei Chen, Tongtong Jin, Binbin Nian and Wenjun Cheng
Molecules 2024, 29(11), 2444; https://doi.org/10.3390/molecules29112444 - 22 May 2024
Viewed by 247
Abstract
Lipases, crucial catalysts in biochemical synthesis, find extensive applications across industries such as food, medicine, and cosmetics. The efficiency of lipase-catalyzed reactions is significantly influenced by the choice of solvents. Polar organic solvents often result in a decrease, or even loss, of lipase [...] Read more.
Lipases, crucial catalysts in biochemical synthesis, find extensive applications across industries such as food, medicine, and cosmetics. The efficiency of lipase-catalyzed reactions is significantly influenced by the choice of solvents. Polar organic solvents often result in a decrease, or even loss, of lipase activity. Conversely, nonpolar organic solvents induce excessive rigidity in lipases, thereby affecting their activity. While the advent of new solvents like ionic liquids and deep eutectic solvents has somewhat improved the activity and stability of lipases, it fails to address the fundamental issue of lipases’ poor solvent tolerance. Hence, the rational design of lipases for enhanced solvent tolerance can significantly boost their industrial performance. This review provides a comprehensive summary of the structural characteristics and properties of lipases in various solvent systems and emphasizes various strategies of protein engineering for non-aqueous media to improve lipases’ solvent tolerance. This study provides a theoretical foundation for further enhancing the solvent tolerance and industrial properties of lipases. Full article
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17 pages, 574 KiB  
Review
Bioremediation of Hazardous Pollutants Using Enzyme-Immobilized Reactors
by Hiroshi Yamaguchi and Masaya Miyazaki
Molecules 2024, 29(9), 2021; https://doi.org/10.3390/molecules29092021 - 27 Apr 2024
Viewed by 599
Abstract
Bioremediation uses the degradation abilities of microorganisms and other organisms to remove harmful pollutants that pollute the natural environment, helping return it to a natural state that is free of harmful substances. Organism-derived enzymes can degrade and eliminate a variety of pollutants and [...] Read more.
Bioremediation uses the degradation abilities of microorganisms and other organisms to remove harmful pollutants that pollute the natural environment, helping return it to a natural state that is free of harmful substances. Organism-derived enzymes can degrade and eliminate a variety of pollutants and transform them into non-toxic forms; as such, they are expected to be used in bioremediation. However, since enzymes are proteins, the low operational stability and catalytic efficiency of free enzyme-based degradation systems need improvement. Enzyme immobilization methods are often used to overcome these challenges. Several enzyme immobilization methods have been applied to improve operational stability and reduce remediation costs. Herein, we review recent advancements in immobilized enzymes for bioremediation and summarize the methods for preparing immobilized enzymes for use as catalysts and in pollutant degradation systems. Additionally, the advantages, limitations, and future perspectives of immobilized enzymes in bioremediation are discussed. Full article
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