Stability Optimization of Biocatalysts (Enzymes)

A Special Issue of Catalysts (ISSN 2073-4344) belonging to the section "Biocatalysis".

Deadline for manuscript submissions: 30 September 2026 | Viewed by 787

Editor


E-Mail Website
Guest Editor
School of Life Science, Beijing Institute of Technology, Beijing 100081, China
Interests: discovery of small molecules; anti-tumor drugs targeting kinase; UPS; associated mechanisms
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Enzymes excel in activity, selectivity, and green credentials, yet their industrial footprint is often limited by their modest operational stability; thermal fluctuations, extreme pH, organic co-solvents, mechanical shear, and product inhibition can rapidly erode catalytic performance, driving up process costs. Recent breakthroughs in protein engineering, immobilization chemistry, formulation science, and in silico design now offer unprecedented opportunities to lock in native structures and functions under harsh reaction conditions.

In this Special Issue, we will collect experimental and computational advances that extend the enzyme lifetime while preserving catalytic efficiency. We welcome the submission of original articles, short communications, and reviews on the following topics:

  1. Directed evolution, rational design, and machine-learning-guided mutagenesis for enhanced rigidity and solvent tolerance.
  2. Novel immobilization matrices (metal–organic frameworks, hierarchical silica, magnetic nanoparticles, bio-based gels) and cross-linking strategies (CLEAs, CLECs, enzyme nanogels).
  3. Post-translational modifications, chemical glycosylation, and ionic liquid or deep eutectic solvent formulations.
  4. Continuous-flow and solid-state biocatalysis, minimizing shear deactivation and facilitating catalyst recycling.
  5. High-throughput stability assays, in situ spectroscopy, and molecular dynamics insights correlating dynamics with deactivation pathways.
  6. Techno-economic and life-cycle assessment of stabilized biocatalysts in pharmaceutical, food, and biofuel applications.

By bridging fundamental protein science with process engineering, in this Special Issue, we aim to define practical routes toward achieving robust, reusable enzymatic systems for sustainable manufacturing

Prof. Dr. Feng Wang
Guest Editor

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 250 words) can be sent to the Editorial Office for assessment.

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-anonymized 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

  • enzyme stability
  • directed evolution
  • immobilization
  • CLEA
  • continuous-flow biocatalysis
  • protein engineering

Benefits of Publishing in a Special Issue

  • Ease of navigation: Grouping papers by topic helps scholars navigate broad scope journals more efficiently.
  • Greater discoverability: Special Issues support the reach and impact of scientific research. Articles in Special Issues are more discoverable and cited more frequently.
  • Expansion of research network: Special Issues facilitate connections among authors, fostering scientific collaborations.
  • External promotion: Articles in Special Issues are often promoted through the journal's social media, increasing their visibility.
  • Reprint: MDPI Books provides the opportunity to republish successful Special Issues in book format, both online and in print.

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

Published Papers (1 paper)

Order results
Result details
Select all
Export citation of selected articles as:

Research

14 pages, 1804 KB  
Article
Efficient Production of 5-Hydroxymethyl-2-Furfurylamine from Expired Beverage Waste via Chemo-Biological Cascade Reaction for Bridging Chemocatalysis and Biocatalysis
by Meizi Huang, Heng Yang and Yu-Cai He
Catalysts 2026, 16(8), 710; https://doi.org/10.3390/catal16080710 - 5 Aug 2026
Viewed by 422
Abstract
In this study, expired beverage (EB) waste was converted into 5-hydroxymethyl-2-furfurylamine (HMFA) through a chemoenzymatic cascade in a malonic acid–choline chloride (MA:ChCl) deep eutectic solvent (DES) system. Under the optimized conditions, HMF was produced from expired beverage waste at 160 °C for 60 [...] Read more.
In this study, expired beverage (EB) waste was converted into 5-hydroxymethyl-2-furfurylamine (HMFA) through a chemoenzymatic cascade in a malonic acid–choline chloride (MA:ChCl) deep eutectic solvent (DES) system. Under the optimized conditions, HMF was produced from expired beverage waste at 160 °C for 60 min using an MA:ChCl-to-EB mass ratio of 1:5. A recombinant Escherichia coli strain co-expressing pyruvate decarboxylase and the engineered ω-transaminase LF was constructed and used to convert EB-derived 5-hydroxymethylfurfural (HMF) into HMFA with a yield of 96.6%. This biological amination of HMF can be conducted under mild conditions via amination (37 °C, 12 h), while reducing the required D-alanine loading (from D-alanine/HMF = 16/1 to D-alanine/HMF = 4/1, based on molar ratio). This two-step chemoenzymatic cascade provides a promising route for producing high-value biofuran compounds from food waste. Full article
(This article belongs to the Special Issue Stability Optimization of Biocatalysts (Enzymes))
Show Figures

Figure 1

Back to TopTop