Advances in Microbial Enzyme Engineering

A special issue of Biology (ISSN 2079-7737). This special issue belongs to the section "Microbiology".

Deadline for manuscript submissions: 31 July 2026 | Viewed by 1027

Special Issue Editors


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Guest Editor
Division of Biotechnology, Faculty of Agro-Industry, Chiang Mai University, Mae-Hea, Muang, Chiang Mai 50100, Thailand
Interests: biotechnology; enzyme engineering and technology; enzymatic applications in biorefinery processes; lignocellulolytic enzymes; proteolytic enzymes; pectinolytic enzymes; protein engineering

E-Mail Website
Guest Editor
Division of Biotechnology, Chiang Mai University, Mae-Hea, Muang, Chiang Mai 50100, Thailand
Interests: biotechnology; enzyme engineering and technology; enzymatic applications in biorefinery processes; lignocellulolytic enzymes; proteolytic enzymes; pectinolytic enzymes; protein engineering

Special Issue Information

Dear Colleagues,

Microbial enzyme engineering has emerged as a pivotal area in biotechnology, offering sustainable and efficient solutions for industrial, agricultural, medical, and environmental applications. Fundamental research in this field focuses on understanding the structure–function relationships of enzymes, elucidating their catalytic mechanisms, and exploring microbial diversity to discover novel enzymes. With the aid of protein engineering, directed evolution, and synthetic biology, researchers can now rationally design or improve enzyme properties, such as stability, specificity, and activity under extreme conditions. Recent advances have also highlighted the importance of metagenomics and systems biology in uncovering uncultivable microbial resources and their enzymatic potential. These developments provide new opportunities to bridge the gap between enzyme discovery and application. This Special Issue welcomes original research articles, reviews, and short communications addressing breakthroughs in microbial enzyme discovery, structure-based enzyme engineering, and functional expression in microbial hosts. Emphasis will be placed on studies that advance our basic understanding of enzyme behavior and provide innovative methodologies that can drive future industrial or biotechnological applications.

Dr. Thanongsak Chaiyaso
Dr. Kamon Yakul
Guest Editors

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Keywords

  • microbial enzyme engineering
  • lignocellulolytic enzymes
  • biorefinery applications
  • protein engineering
  • enzyme-based biomass conversion
  • synthetic biology

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Published Papers (1 paper)

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Research

15 pages, 1329 KB  
Article
Engineering the Bacterial Laccase CotA for Functional Expression and Dye Decolorization Through Site-Directed Mutagenesis
by Zhiguo Zhou, Shuyuan Yao, Sitie Ying, Mengyan Yu, Zhihua Song, Yongtao Sun, Lisheng Qian and Yue Zhang
Biology 2025, 14(10), 1335; https://doi.org/10.3390/biology14101335 - 28 Sep 2025
Viewed by 299
Abstract
The relationship between the structure and function of bacterial laccases has garnered significant research attention thanks to their straightforward molecular structure. Nevertheless, studies examining the impact of an altered molecular structure on the heterologous expression of bacterial laccases in Escherichia coli remain scarce. [...] Read more.
The relationship between the structure and function of bacterial laccases has garnered significant research attention thanks to their straightforward molecular structure. Nevertheless, studies examining the impact of an altered molecular structure on the heterologous expression of bacterial laccases in Escherichia coli remain scarce. Our research focuses on elucidating the impact of incorporating copper ions into the molecular structure of modified CotA on its exogenous expression in E. coli as well as its impact on the significance of the amino acid residues surrounding the internal electron channels and water molecule channels of the enzyme molecule. The results show that single-site mutation may affect the expression of CotA by affecting its soluble expression with different binding capacities for copper ions. In addition, the mutants exhibited different laccase activity levels. The catalytic efficiency of T466A was found to be significantly enhanced, reaching 2.29 times that of the wild type. We used structural models to illustrate the correlation between molecular structure and function after the replacement of three mutation sites with alanine. The reduction of hydrogen bonds may be an important factor influencing Cu2+’s binding ability and the water molecule production rate. The T466A mutant exhibited strong decolorization ability for Reactive Blue 19 and Eriochrome Black T with 42.2% and 58.2% decolorization rates after one hour of reaction, respectively. This study demonstrates that the molecular mutation studied influences the CotA expression level, enzyme activity, and dye decolorization. Full article
(This article belongs to the Special Issue Advances in Microbial Enzyme Engineering)
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