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 10
Special Issue Editors
Interests: biocatalysis; industrial biotechnology; lignocellulose degrading enzymes; novel enzymes; structure-function relationship
Special Issues, Collections and Topics in MDPI journals
Interests: heterogeneous biocatalysts; enzyme stabilization; flow microreactor; process intensification
Special Issues, Collections and Topics in MDPI journals
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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