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Catalysts
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Biocatalysis-Driven Catalytic Routes for Green and Alternative Chemical Production
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Biocatalysis-Driven Catalytic Routes for Green and Alternative Chemical Production

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

Deadline for manuscript submissions: 30 December 2026 | Viewed by 2047

Special Issue Editors

Dr. Kaili Nie

E-Mail Website
Guest Editor
Beijing Key Laboratory of Bioprocess, National Energy R&D Center for Biorefinery, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, China
Interests: enzymes; biocatalysis; enzyme engineering; directed evolution; rational design; metabolic engineering
Special Issues, Collections and Topics in MDPI journals
Dr. Junfeng Liu

E-Mail Website
Guest Editor
Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, China
Interests: metabolic engineering; synthetic biology; enzymes; multi-omics analysis

Special Issue Information

Dear Colleagues,

Biocatalysis is increasingly transforming chemical manufacturing by delivering unmatched chemo-, regio-, and stereoselectivity under mild conditions. However, broader industrial adoption requires new catalytic routes that replace energy-intensive, wasteful, or hazardous conventional processes while expanding accessible reactivity. This Special Issue highlights biocatalysis-centered transformations for green and alternative chemical production, with an emphasis on coupling enzymes with complementary catalytic modes to unlock synergistic performance. We welcome original articles and critical reviews covering, but not limited to, enzyme-led coupled, tandem, and cascade processes; chemoenzymatic systems integrating enzymes with metal catalysis (homogeneous, heterogeneous, or biohybrid); and photobiocatalysis and enzyme–photocatalyst coupling for novel bond formations and selective redox chemistry. We also seek submissions on electrobiocatalysis and enzyme–electrocatalyst coupling for cofactor regeneration and redox-intensive conversions, as well as integrated one-pot and flow processes, immobilization, and process intensification. Contributions that demonstrate credible greener alternatives to established synthetic routes—supported by mechanistic insight, quantitative sustainability metrics, and/or scalable process concepts—are particularly encouraged.

If you would like to submit papers to this Special Issue or have any questions, please contact the in-house editor, Ms. Rita Lin (rita.lin@mdpi.com).

Dr. Kaili Nie
Dr. Junfeng Liu
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 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-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

  • enzyme
  • enzyme catalysis
  • biocatalysis
  • cascade processes
  • chemoenzymatic systems
  • process intensification
  • green synthesis technology
  • green and alternative chemical production

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Published Papers (3 papers)

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Research

18 pages, 8452 KB  
Article
Chemoenzymatic Two-Step Synthesis of Albendazole–Cholic Acid Conjugates: Linker-Length-Controlled Biocatalytic Esterification
by Shuyi Shang, Jiahao Liu, Jingshuai Liu, Zhimei Guo, Shuming Jin, Chunhui Hu, Fabin Zhang and Kaili Nie
Catalysts 2026, 16(5), 382; https://doi.org/10.3390/catal16050382 - 27 Apr 2026
Viewed by 275
Abstract
Albendazole (ABZ) exhibits poor oral absorption; therefore, ABZ was conjugated to cholic acid to engage the apical sodium-dependent bile acid transporter (ASBT) and promote ileal uptake. ABZ–linker–CA conjugates bearing amino-alcohol linkers (C4–C8) were evaluated by integrating synthetic feasibility, purification selectivity, and ex vivo [...] Read more.
Albendazole (ABZ) exhibits poor oral absorption; therefore, ABZ was conjugated to cholic acid to engage the apical sodium-dependent bile acid transporter (ASBT) and promote ileal uptake. ABZ–linker–CA conjugates bearing amino-alcohol linkers (C4–C8) were evaluated by integrating synthetic feasibility, purification selectivity, and ex vivo performance. Thermal aminolysis in DMF (95 °C) produced ABZ–linkers in ~50% reaction yields (HPLC-assayed), with a minor ABZ-amine by-product consistent with a workup-sensitive isocyanate route. Immobilized-lipase screening identified Lipozyme RM IM as the most effective catalyst for CA esterification in CHCl3, showing a pronounced linker-length dependence (31% yield for C4, 25% for C6, and C8 ≤ 2.6% yield). Docking and molecular dynamics supported this trend by indicating productive binding geometries for C4/C6 but not for C8. A polarity-guided workup and silica-gel protocol enabled retrieval of unreacted intermediates and CA recycling, with cleaner separation for the C6 series. Ex vivo transport studies confirmed ASBT-mediated, linerixibat-sensitive ileal uptake, and protoscolex assays showed improved antiparasitic efficacy versus ABZ. Overall, ABZ-C6-CA offered the best balance of uptake, near-maximal efficacy, enzymatic accessibility, and separability, supporting its prioritization for scalable biocatalytic manufacturing. Full article
(This article belongs to the Special Issue Biocatalysis-Driven Catalytic Routes for Green and Alternative Chemical Production)
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20 pages, 921 KB  
Article
ThermoFormer: Predicting Protein Melting Temperature Through Large-Scale Pretraining
by Jingchuan Li and Mingchen Li
Catalysts 2026, 16(4), 288; https://doi.org/10.3390/catal16040288 - 24 Mar 2026
Viewed by 747
Abstract
Temperature plays a dominant environmental role in determining the efficiency of protein function. Accurately predicting protein thermal stability is crucial for fundamental biology, drug discovery, and protein engineering. Here, we introduce ThermoFormer, a transformer-based protein language model that learns both temperature-aware representation and [...] Read more.
Temperature plays a dominant environmental role in determining the efficiency of protein function. Accurately predicting protein thermal stability is crucial for fundamental biology, drug discovery, and protein engineering. Here, we introduce ThermoFormer, a transformer-based protein language model that learns both temperature-aware representation and sequence patterns. Specifically, we first built a large-scale dataset comprising more than 96 million protein sequences annotated with their optimal growth temperature (OGT). ThermoFormer is pre-trained with a supervised OGT prediction task and an unsupervised masked language modeling (MLM) task on the dataset. We evaluated ThermoFormer’s pre-training performance and its transferability to other temperature-prediction datasets, including two melting temperature (TM) datasets, an optimal catalytic temperature (OCT) dataset, and a thermophilic protein classification task. The results show that ThermoFormer achieves state-of-the-art performance across all evaluated tasks, outperforming prior unsupervised pre-trained models. In addition, we have also shown that ThermoFormer enables zero-shot temperature prediction, i.e., even without further fine-tuning, ThermoFormer can still achieve comparable performance. Our model can serve as a foundation for encoding protein sequences with temperature-aware representations, improving transferability to temperature-related downstream tasks. Full article
(This article belongs to the Special Issue Biocatalysis-Driven Catalytic Routes for Green and Alternative Chemical Production)
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14 pages, 1722 KB  
Article
A Two-Enzyme Entry Module Triggers an Endogenous Biocatalytic Cascade for Green Biosynthesis of Pyridoxal 5′-Phosphate in Corynebacterium glutamicum
by Li Qi, Hao He, Shihao Xiang and Hui Cao
Catalysts 2026, 16(2), 195; https://doi.org/10.3390/catal16020195 - 20 Feb 2026
Viewed by 688
Abstract
Pyridoxal 5′-phosphate (PLP), the active form of vitamin B6, is an essential cofactor, yet its industrial supply still relies largely on multi-step chemical synthesis. Here, using the industrial chassis Corynebacterium glutamicum ATCC 13032, we proposed and validated a strategy based on a minimal [...] Read more.
Pyridoxal 5′-phosphate (PLP), the active form of vitamin B6, is an essential cofactor, yet its industrial supply still relies largely on multi-step chemical synthesis. Here, using the industrial chassis Corynebacterium glutamicum ATCC 13032, we proposed and validated a strategy based on a minimal heterologous entry coupled to endogenous pathway continuation, resulting in a distinct PLP-producing route. Three engineered strains were constructed and compared: S1 expressing ecepd from Escherichia coli; S2 co-expressing ecepd plus ecpdxB from Escherichia coli (a minimal two-gene module); and S3 carrying an additional ecpdxA from Escherichia coli and smpdxJ from Sinorhizobium meliloti to form a four-gene module as a benchmark for heterologous reconstruction. The wild-type (WT) strain produced a basal PLP level of 10.6 mg/L. Overexpressing ecepd alone increased the titer to 40.4 mg/L (3.8-fold vs WT), whereas the minimal two-gene module in S2 yielded the highest PLP titer of 95.5 mg/L (9.0-fold vs WT; 136.0% higher than S1). Notably, the four-gene module (S3) reached 70.0 mg/L, which was 36.3% lower than S2 under matched conditions. These results indicated that introducing only a minimal two-gene entry could cooperate with the endogenous metabolic network of Corynebacterium glutamicum to establish a new and highly effective PLP biosynthetic route, with production performance exceeding that of a multi-gene heterologous reconstruction in the tested window. This work provides a low-burden and scalable framework for sustainable PLP biomanufacturing and motivates further optimization targeting the endogenous continuation steps and regulatory constraints. Full article
(This article belongs to the Special Issue Biocatalysis-Driven Catalytic Routes for Green and Alternative Chemical Production)
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