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New Trends in Industrial Biocatalysis, 2nd Edition
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New Trends in Industrial Biocatalysis, 2nd Edition

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

Deadline for manuscript submissions: 15 August 2025 | Viewed by 5034

Special Issue Editors

Prof. Dr. Rosa María Oliart-Ros

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Guest Editor
Unidad de Investigación y Desarrollo en Alimentos, Tecnológico Nacional de México/Instituto Tecnológico de Veracruz, Veracruz 91897, Mexico
Interests: extremozymes; extremophiles; biocatalysis; lipolytic enzymes; metagenomics
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. María Guadalupe Sánchez-Otero

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Guest Editor
Facultad de Bioanálisis, Universidad Veracruzana, Veracruz 91000, Mexico
Interests: extremophiles; extremozymes; biocatalysis; lipases; enzyme immobilization
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

This Special ssue is a continuation of the previous successful Special Issue “New Trends in Industrial Biocatalysis”.

Today, industrial biocatalysis is particularly important for industrial biotechnology because it uses environmentally friendly, cost-effective, and sustainable processes. The improvement of these processes involves the screening and isolation of novel biocatalysts with new properties and capacities, which can be undertaken by metagenomic approaches or classical isolation techniques, as well as the improvement of their performance by emerging techniques such as the production of immobilized and co-immobilized preparations on new matrices, the enhancement of enzymatic capacities through mutagenesis and directed evolution, accompanied by in silico prediction studies and structural elucidation of biomolecules. Other areas of interest comprise the discovery of new reactions/products or the optimization of existing ones by the use of non-conventional substrates and/or solvents, with applications in the pharmaceutical and food industries as prominent examples.

This Special Issue, “New Trends in Industrial Biocatalysis, 2nd Edition”, intends to compile the most recent developments, techniques, and practices in the field of industrial biocatalysis. We encourage scientists working in biocatalysis, enzymatic biotechnology, and extremophilic enzymes applied in biocatalysis to publish their recent findings and results in areas such as enzyme, protein, and medium engineering for the improvement or establishment of biocatalytic processes; new nanomaterials, nanofibers, polymers, and mesoporous materials such as MOFs to immobilize enzymes and improve catalytic functions; novel modifications in immobilization solid support; new biocatalytic strategies to treat effluents; new strategies for cofactor recycling; and the design and use of flow reactors or solid-state reactors in biocatalysis.

Prof. Dr. Rosa María Oliart-Ros
Prof. Dr. María Guadalupe Sánchez-Otero
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

  • industrial biocatalysis
  • extremozymes
  • immobilization
  • metal–organic frameworks
  • covalent–organic frameworks
  • protein engineering
  • mutagenesis

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Related Special Issue

Published Papers (4 papers)

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Research

Jump to: Review

19 pages, 10816 KiB  
Article
Self-Assembly of Benzyloxycarbonyl Histidine with Zinc Ions for the Construction of Esterase Mimics
by Jiacheng Sun, Jingjing Guo, Ling Liu, Yu Liu, Linling Yu and Yan Sun
Catalysts 2025, 15(2), 185; https://doi.org/10.3390/catal15020185 - 17 Feb 2025
Viewed by 638
Abstract
Esterases have been applied in many industrial fields. However, many esterases have inherent defects as natural enzyme, such as low long-term storability, poor operational stability, and difficulty in recovery for reuse. Herein, two histidine derivatives with different structures, L-benzyloxycarbonyl histidine (Z-L-His) and D-benzyloxycarbonyl [...] Read more.
Esterases have been applied in many industrial fields. However, many esterases have inherent defects as natural enzyme, such as low long-term storability, poor operational stability, and difficulty in recovery for reuse. Herein, two histidine derivatives with different structures, L-benzyloxycarbonyl histidine (Z-L-His) and D-benzyloxycarbonyl histidine (Z-D-His), were used to self-assemble with zinc ions to construct esterase mimics (Z-L-His/Zn2+ and Z-D-His/Zn2+) based on a minimalist strategy. Two natural enzymes were used for comparison. It was found that the Z-His structure influenced only the stereoselectivity of the enzyme mimic. The kinetics of Z-L-His/Zn2+ followed the classical Michaelis–Menten equation, and its catalytic efficiency was comparable to that of natural enzymes. It was verified that Z-L-His/Zn2+ had good catalytic stability over a wide range of pH, organic solvent concentrations, ionic strengths, and incubation temperatures. Z-L-His/Zn2+ retained high activity after incubation in different environments for 7 d, demonstrating excellent long-term storage stability. Moreover, Z-L-His/Zn2+ exhibited good reusability, retaining 93% of its original activity after six cycles, proving its potential for industrial applications in mimicking esterase. Full article
(This article belongs to the Special Issue New Trends in Industrial Biocatalysis, 2nd Edition)
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22 pages, 3391 KiB  
Article
Enantioselectivity Enhancement of a Geobacillus thermoleovorans CCR11 Lipase by Rational Design
by Aaron-Salvador Bustos-Baena, Rodolfo Quintana-Castro, María Guadalupe Sánchez-Otero, Graciela Espinosa-Luna, María Remedios Mendoza-López, Carolina Peña-Montes and Rosa María Oliart-Ros
Catalysts 2025, 15(2), 168; https://doi.org/10.3390/catal15020168 - 12 Feb 2025
Cited by 2 | Viewed by 873
Abstract
Lipases are enzymes that catalyze the hydrolysis of carboxylic esters at a lipid–water interface and are able to catalyze reactions such as alcoholysis, esterification, transesterification, and enantioselective synthesis in organic media. They are important biocatalysts for biotechnological and industrial applications—such as in the [...] Read more.
Lipases are enzymes that catalyze the hydrolysis of carboxylic esters at a lipid–water interface and are able to catalyze reactions such as alcoholysis, esterification, transesterification, and enantioselective synthesis in organic media. They are important biocatalysts for biotechnological and industrial applications—such as in the food and flavor industry—and in the production of biopharmaceuticals, biofuels, biopolymers, and detergents. A desirable property of lipases is stereoselectivity for the production of chemicals with high optical purity. In this work, we report the improvement of the enantioselective capabilities of the Geobacillus thermoleovorans CCR11 lipase. By means of a rational design and bioinformatic approaches, six amino acids of the catalytic cavity of the lipase LipTioCCR11 were substituted resulting in an increase in the optimum temperature of the enzyme and in the resistance to the presence of organic solvents in hydrolytic reactions, and in the promotion of the enantioselective recognition of R isomers of carboxylic acids with importance for the pharmaceutical and food industries. Full article
(This article belongs to the Special Issue New Trends in Industrial Biocatalysis, 2nd Edition)
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Review

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14 pages, 4640 KiB  
Review
Strategies and Recent Trends in Engineering Thermostable GH11 Xylanases
by Beom Soo Kim and In Jung Kim
Catalysts 2025, 15(4), 317; https://doi.org/10.3390/catal15040317 - 26 Mar 2025
Viewed by 584
Abstract
Glycoside hydrolase family 11 (GH11) xylanases are used in various industries, such as biorefining, animal feed production, and baking, making them key industrial enzymes. Operating bioprocesses at elevated temperatures enhances the reaction rate and product yield and thus requires thermostable enzymes to sustain [...] Read more.
Glycoside hydrolase family 11 (GH11) xylanases are used in various industries, such as biorefining, animal feed production, and baking, making them key industrial enzymes. Operating bioprocesses at elevated temperatures enhances the reaction rate and product yield and thus requires thermostable enzymes to sustain catalytic performance. The limited availability of naturally occurring thermostable GH11 xylanases necessitates targeted modifications via protein engineering to enhance their thermal stability. In this review, we present the key drivers of thermostability, an overview of engineering strategies, and the underlying mechanisms of action. Finally, we investigated state-of-the-art technologies involving artificial intelligence (AI)- and ancestral sequence reconstruction-guided approaches. Full article
(This article belongs to the Special Issue New Trends in Industrial Biocatalysis, 2nd Edition)
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17 pages, 12770 KiB  
Review
Engineering Xylose Isomerase for Industrial Applications
by Ki Hyun Nam
Catalysts 2024, 14(9), 597; https://doi.org/10.3390/catal14090597 - 5 Sep 2024
Cited by 1 | Viewed by 2421
Abstract
Xylose isomerase (XI), also known as glucose isomerase, is an aldose isomerase that converts D-glucose to D-fructose and D-xylose to D-xylulose. This enzyme is widely used in the production of high-fructose corn syrup and bioethanol. Enhancing the efficiency of XI is critical for [...] Read more.
Xylose isomerase (XI), also known as glucose isomerase, is an aldose isomerase that converts D-glucose to D-fructose and D-xylose to D-xylulose. This enzyme is widely used in the production of high-fructose corn syrup and bioethanol. Enhancing the efficiency of XI is critical for its use in industrial applications. To improve the enzymatic efficiency of XI in the desired reaction environment, various protein engineering studies have used rational engineering and directed evolution. This review introduces the molecular features and structural studies of XI. Additionally, it provides a structural analysis of the functional characteristics of the engineering sites discovered through biochemical and computational experiments in engineered XI research. This review will offer crucial insights for future XI engineering aimed at enhancing its industrial applications. Full article
(This article belongs to the Special Issue New Trends in Industrial Biocatalysis, 2nd Edition)
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