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Catalysts
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15th Anniversary of Catalysts: The Future of Enzyme Biocatalysis
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15th Anniversary of Catalysts: The Future of Enzyme Biocatalysis

A special issue of Catalysts (ISSN 2073-4344).

Deadline for manuscript submissions: 30 April 2026 | Viewed by 754

Special Issue Editors

Prof. Dr. Evangelos Topakas

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Guest Editor
Biotechnology Laboratory, School of Chemical Engineering, National Technical University of Athens, 9 Iroon Polytech Str, Zografou Campus, 15780 Athens, Greece
Interests: biocatalysis; industrial biotechnology; lignocellulose degrading enzymes; novel enzymes; structure-function relationship
Special Issues, Collections and Topics in MDPI journals
Dr. Juan M. Bolivar

E-Mail Website
Guest Editor
Department of Chemical Engineering, School of Chemical Sciences, Complutense University of Madrid, Madrid, Spain
Interests: heterogeneous biocatalysts; enzyme stabilization; flow microreactor; process intensification
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Chia-Hung Kuo

E-Mail Website
Guest Editor
Department of Seafood Science, National Kaohsiung University of Science and Technology, Kaohsiung 81157, Taiwan
Interests: food analysis; food processing; cellulase; lipase esterification and trans esterification; amylase; enzymatic kinetics; ultrasound-assisted enzymatic reaction; enzyme extraction; biotransformation; saccharification; response surface methodology; artificial neural network; wine fermentation
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Celebrating the 15th anniversary of the Catalysts journal, this Special Issue marks the sustained growth and evolving impact of the Biocatalysis section within the journal. As demonstrated in our Biocatalysis section, enzyme or whole-cell biocatalysis has transitioned from a specialized niche into a central technology for sustainable synthesis and analysis, with over 1000 articles and dozens of dedicated Special Issues to date.

In this anniversary edition, we aim to reflect on historical successes while focusing on frontier developments redefining the field today: advances in machine‑learning‑guided enzyme design, photobiocatalysis, enzymatic cascade engineering, enzyme immobilization for continuous flow, and expanding chemoenzymatic approaches in green chemistry. We encourage contributions that challenge traditional paradigms, propose novel strategies for enzyme discovery and stability, and illustrate industrial translation of emerging tools.

Authors are invited to submit both original research and critical reviews exploring grand themes in biocatalysis—particularly those that harness synthetic biology, artificial intelligence, and process intensification. This collection aims to chart the future trajectory of enzyme or whole-cell catalysis for green synthesis, biomanufacturing, and beyond. We look forward to your innovative contributions.

Prof. Dr. Evangelos Topakas
Dr. Juan M. Bolivar
Prof. Dr. Chia-Hung Kuo
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

  • machine‑learning enzyme design
  • photobiocatalysis
  • immobilized enzymes and flow bioprocesses
  • directed evolution and computational enzyme engineering
  • biocatalysis in sustainable chemical production
  • emerging enzyme classes and non‑natural transformations

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Published Papers (1 paper)

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Research

25 pages, 3623 KB  
Article
Fusarium proliferatum PSA-3 Produces Xylanase-Aggregate to Degrade Complex Arabinoxylan
by Kanlaya Thattha, Lakha Salaipeth, Saengchai Akeprathumchai, Ken-Lin Chang, Takashi Watanabe and Paripok Phitsuwan
Catalysts 2025, 15(10), 988; https://doi.org/10.3390/catal15100988 - 16 Oct 2025
Viewed by 567
Abstract
Xylanolytic enzymes of the Fusarium species are closely associated with pathogenesis, where they soften plant cell walls to facilitate infection and nutrient uptake. This study investigated the xylanolytic system of Fusarium proliferatum PSA-3, a strain isolated from mango leaves showing dark spot symptoms. [...] Read more.
Xylanolytic enzymes of the Fusarium species are closely associated with pathogenesis, where they soften plant cell walls to facilitate infection and nutrient uptake. This study investigated the xylanolytic system of Fusarium proliferatum PSA-3, a strain isolated from mango leaves showing dark spot symptoms. When cultivated on rice straw under solid-state fermentation, PSA-3 produced high xylanase activity against rye arabinoxylan (50.2 U) and beechwood xylan (56.8 U). Partial purification by ion-exchange and gel-filtration chromatography yielded a large xylanase aggregate (158 kDa), which appeared as a smear at the top of the gel under native conditions. Mild denaturation resolved the aggregate into at least four active proteins of ~25, 35, 48, and 63 kDa, indicating that multiple xylanases assemble into a functional aggregate. The aggregate retained activity across pH 4.0–8.0, with an optimum at pH 5.0 and 50 °C, and was resistant to Ni2+, Fe2+, Co2+, and β-mercaptoethanol, but inhibited by SDS. Hydrolysis of xylo-oligosaccharides (DP 2–6), purified xylans, and plant-derived xylans confirmed predominantly endo-type action with debranching activity toward A2XX and A2,3XX. These findings reveal a natural xylanase aggregate in F. proliferatum, providing a potential mechanism for efficient degradation of arabinoxylan-rich cell walls and offering targets for antifungal strategies and biotechnological applications. Full article
(This article belongs to the Special Issue 15th Anniversary of Catalysts: The Future of Enzyme Biocatalysis)
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