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: 30 November 2025 | Viewed by 631

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School of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, China
Interests: nanocomposite; bio-based materials; synthesis; modification; characterization
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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

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Keywords

  • enzyme engineering
  • enzyme kinetics and optimization
  • industrial biotechnology
  • industrial microbiology
  • microbial metabolism

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Published Papers (1 paper)

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Research

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 361
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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