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Biomolecules
Special Issues
Industrial Microorganisms and Enzyme Technologies
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Industrial Microorganisms and Enzyme Technologies

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Enzymology".

Deadline for manuscript submissions: 20 May 2026 | Viewed by 5781

Special Issue Editor

Prof. Dr. Yunjun Yan

E-Mail Website
Guest Editor
School of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, China
Interests: nanocomposite; bio-based materials; synthesis; modification; characterization
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Industrial microorganisms and enzyme technologies play a pivotal role in modern biotechnology, driving innovations in sustainable manufacturing, bioenergy, pharmaceuticals, food production, etc. Advances in genetic engineering, synthetic biology, and biocatalysis have significantly enhanced the efficiency and scalability of microbial and enzymatic processes. These technologies are critical for reducing environmental impacts, lowering production costs, and enabling the transition toward a circular bioeconomy.

This Special Issue aims to compile high-quality research on the digging, optimization, engineering, and application of industrial microbes and enzymes for biotechnological and industrial processes. By focusing on both fundamental and applied studies, this Special Issue will provide insights into novel strategies for strain improvement, enzyme design, metabolic engineering, and bioprocess optimization. The topic aligns with the journal’s scope of advancing sustainable and innovative biotechnological solutions.

In this Special Issue, original research articles and reviews are both welcome. Research areas may include (but are not limited to) the following:

  • Microbial strain development and metabolic engineering;
  • Enzyme discovery, engineering, and immobilization;
  • Bioprocess optimization and scale-up;
  • Applications in biofuels, bioremediation, and green chemistry;
  • Synthetic biology tools for industrial microorganisms;
  • Computational modeling of microbial and enzyme systems.

We look forward to receiving your contributions.

Prof. Dr. Yunjun Yan
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-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biomolecules 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 2700 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 engineering
  • enzyme kinetics and optimization
  • industrial biotechnology
  • industrial microbiology
  • microbial metabolism

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

Published Papers (4 papers)

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Research

16 pages, 2075 KB  
Article
Comparative Transcriptomics Reveals the Molecular Basis for Inducer-Dependent Efficiency in Gastrodin Propionylation by Aspergillus oryzae Whole-Cell Biocatalyst
by Desheng Wu, Maohua Ma, Xiaohan Liu, Xiaofeng Li and Guanglei Zhao
Biomolecules 2025, 15(12), 1695; https://doi.org/10.3390/biom15121695 - 4 Dec 2025
Viewed by 591
Abstract
Propionylated derivatives of gastrodin are valuable due to their enhanced lipophilicity and bioavailability. This study investigated the molecular basis for the differential catalytic efficiency of Aspergillus oryzae whole cells in gastrodin propionylation. A high conversion rate of 96.84% was achieved with soybean oil [...] Read more.
Propionylated derivatives of gastrodin are valuable due to their enhanced lipophilicity and bioavailability. This study investigated the molecular basis for the differential catalytic efficiency of Aspergillus oryzae whole cells in gastrodin propionylation. A high conversion rate of 96.84% was achieved with soybean oil induction, compared to only 8.23% under glucose induction. Comparative transcriptomic analysis identified 20,342 differentially expressed genes (DEGs), which were significantly enriched in lipid metabolism and signal transduction pathways. From 26 upregulated lipase-related DEGs, a candidate triacylglycerol lipase gene (CL24.Contig40_All) was prioritized. Homology modeling and molecular docking supported its potential role by demonstrating that the encoded enzyme possesses a typical α/β hydrolase fold with a catalytic triad and favorable binding with both gastrodin and vinyl propionate. These findings indicate that soybean oil may enhance lipase expression by activating lipid metabolic and phosphatidylinositol signaling pathways, providing crucial transcriptional-level insights and genetic targets for the rational design of efficient whole-cell biocatalysts. Full article
(This article belongs to the Special Issue Industrial Microorganisms and Enzyme Technologies)
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21 pages, 3319 KB  
Article
High-Intensity Pulse Magnetic Fields Affect Redox Homeostasis and Survival Rate of Escherichia coli According to Initial Level of Intracellular Glucose
by Pengbo Wang, Limeng Du, Yunchong Li, Zitang Xu, Luona Ye, Shuhan Dai, Li Xu, Jinyong Yan, Xiaoman Xie, Quanliang Cao, Min Yang, Xiaotao Han and Yunjun Yan
Biomolecules 2025, 15(11), 1550; https://doi.org/10.3390/biom15111550 - 5 Nov 2025
Cited by 1 | Viewed by 930
Abstract
The biological effects of magnetic fields (MFs) have been studied and applied in medicine over the past four decades. However, the influence of high-intensity pulse magnetic fields (HI-PMFs), theorized to exert even stronger biological effects, is rarely reported. Herein, a study was conducted [...] Read more.
The biological effects of magnetic fields (MFs) have been studied and applied in medicine over the past four decades. However, the influence of high-intensity pulse magnetic fields (HI-PMFs), theorized to exert even stronger biological effects, is rarely reported. Herein, a study was conducted to investigate the biological effects of 2.5 T HI-PMF on the model organism Escherichia coli and its corresponding physiological alterations. After being treated by HI-PMF, a notable increase was observed in its intracellular NADH/NAD+ ratio, coupled with an improved cell survival rate. Transcriptome analysis revealed significant upregulation of genes related to glucose metabolism. Subsequent experiments confirmed that if the initial intracellular glucose level was relatively high and markedly decreased after being treated with HI-PMF, the cell density would significantly rise, owing to the alleviated inhibition of cell division. On the contrary, a lower initial intracellular glucose level led to cell death under HI-PMF. Furthermore, reactive oxygen species (ROS) production was proved to be the main cause attributed to the above phenomena. Therefore, our study suggests that HI-PMF treatment promotes ROS production, enhances cellular glucose metabolism, and consequently influences cell division and survival rate according to the initial level of intracellular glucose. Full article
(This article belongs to the Special Issue Industrial Microorganisms and Enzyme Technologies)
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25 pages, 6307 KB  
Article
A Highly Active Keratinase from Bacillus sp. FJ-3-16 for Sustainable Feather Waste Valorization and Eco-Friendly Industrial Applications
by Fei Bian, Hailun He, Gao Chen, Shousong Yue, Yaoxia Zhu, Xiaowei Zhang and Bin-Bin Xie
Biomolecules 2025, 15(10), 1389; https://doi.org/10.3390/biom15101389 - 29 Sep 2025
Cited by 2 | Viewed by 2354
Abstract
Keratinous biomass, such as feathers, wool, and hair, poses environmental challenges due to its insoluble and recalcitrant nature. In this study, we identified, purified and comprehensively characterized a previously uncharacterized extracellular alkaline keratinase, KerFJ, secreted by Bacillus sp. FJ-3-16, with broad industrial application [...] Read more.
Keratinous biomass, such as feathers, wool, and hair, poses environmental challenges due to its insoluble and recalcitrant nature. In this study, we identified, purified and comprehensively characterized a previously uncharacterized extracellular alkaline keratinase, KerFJ, secreted by Bacillus sp. FJ-3-16, with broad industrial application potential. KerFJ was produced at high yield (1800 U/mL) in an optimized cost-effective medium and purified to homogeneity using ion-exchange chromatography. The enzyme exhibited optimal activity at pH 9.5 and 55 °C, with remarkable alkaline and thermal stability, and high tolerance to surfactants, oxidants, and metal ions. Sequence analysis revealed that KerFJ is a member of the serine peptidase S8 family, with a molecular weight of ~27.5 kDa. It efficiently degraded native keratin substrates, achieving 70.3 ± 2.1% feather, 39.7 ± 1.8% wool, and 15.4 ± 1.2% hair degradation, and the resulting feather hydrolysates exhibited strong antioxidant activities. KerFJ also demonstrated excellent compatibility with commercial detergents and enabled effective stain removal from fabrics without damage. Moreover, both laboratory- and pilot-scale trials showed that KerFJ facilitated non-destructive dehairing of sheep, donkey, and pig skins while preserving collagen integrity. These results highlight KerFJ as a robust and multifunctional biocatalyst suitable for keratin waste valorization, eco-friendly leather processing, and detergent formulations. Full article
(This article belongs to the Special Issue Industrial Microorganisms and Enzyme Technologies)
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14 pages, 2944 KB  
Article
Improvement of Soluble Expression, Stability, and Activity of Acetaldehyde Lyase by Elastin-like Polypeptides Fusion for Acetoin Production from Acetaldehyde
by Hui Lin, Jiming Zhang, Jie Hu, Lu Ma, Kaili Lai, Chaosong Zheng, Qiuhua Yang and Liaoyuan Zhang
Biomolecules 2025, 15(9), 1216; https://doi.org/10.3390/biom15091216 - 22 Aug 2025
Viewed by 1243
Abstract
To achieve the large-scale, low-cost preparation of acetaldehyde lyase (ALS), elastin-like polypeptides (ELPs) as non-chromatographic purification tags were employed to develop an ELP-ALS fusion protein in Escherichia coli. Induction expression results demonstrated that the ELPs tag efficiently improved the soluble expression of [...] Read more.
To achieve the large-scale, low-cost preparation of acetaldehyde lyase (ALS), elastin-like polypeptides (ELPs) as non-chromatographic purification tags were employed to develop an ELP-ALS fusion protein in Escherichia coli. Induction expression results demonstrated that the ELPs tag efficiently improved the soluble expression of the ALS enzyme. Through two rounds of inverse transition cycling (ITC), highly pure ELP-ALS was obtained with an enzyme recovery rate of 85.77%, outperforming Ni2+-affinity chromatography (66.80%). The comparative analysis of enzymatic properties revealed that ELP fusion markedly improved the stability and substrate tolerance of the ALS enzyme. Kinetic parameter analysis under identical conditions showed that ELP-ALS possessed a Vmax of 15.25 U/mg and a kcat/Km of 73.05 s−1·M−1, representing 1.86-fold and 2.97-fold improvements over His-ALS, respectively. Fed-batch reaction using ELP-ALS and acetaldehyde as biocatalyst and substrate, respectively, yielded 95.92 g/L acetoin with 49.32% increase compared to His-ALS (64.24 g/L). These results demonstrated the application potential of ELP-ALS as a promising biocatalyst for acetoin production from acetaldehyde due to its lower preparation cost, higher biocatalytic efficiency, better stability, and substrate tolerance. Full article
(This article belongs to the Special Issue Industrial Microorganisms and Enzyme Technologies)
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