The Improvement of Biocatalysis: Enzyme and Reaction Medium Modification

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

Deadline for manuscript submissions: closed (15 July 2023) | Viewed by 3324

Special Issue Editors


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Guest Editor
Jerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Niezapominajek 8, 30-239 Krakow, Poland
Interests: metalloenzymes; catalytic mechanisms; enzymes from anaerobic metabolic pathways; modelling enzymatic reactions; reaction engineering
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Guest Editor
Department of Process Engineering, Equipment and Food Biotechnology, University of Warmia and Mazury in Olsztyn, Jan Heweliusz St. 1, 10-718 Olsztyn, Poland
Interests: food enzymes; biocatalysis; medium engineering; food compounds modification; enzyme inhibition; lignocellulose hydrolysis; fermentation
Special Issues, Collections and Topics in MDPI journals

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Guest Editor
Department of Process Engineering, Equipment and Food Biotechnology, University of Warmia and Mazury in Olsztyn, Jan Heweliusz St. 1, 10-718 Olsztyn, Poland
Interests: enzymatic modification of food ingredients; food enzymes; reaction environmental engineering; enzymes in reduction of food immunoreactivity; fermentation

Special Issue Information

Dear Colleagues,

Chemical reactions catalyzed by enzymes are important because of the rate and stereospecificity of transformation. Biocatalysts are a greener alternative to traditional synthesis that offers a tool for the transformation under mild reaction conditions, low energy requirements and minimizing the problems of isomerization and rearrangement. However, the application of enzymes is often limited because of the harsh reaction medium conditions, and the use of non-conventional solvents. In recent decades, a new paradigm of biocatalysis was presented to overcome enzyme deactivation or a dramatic drop in catalytic activity. The new paradigm required modification and matching of enzyme properties to bioprocess requirements. The target is the development of tailor-made biocatalysts suitable for industrial applications. Detailed molecular understanding of the protein structure and conformational dynamics allows us to tune catalytic activity by modifying the solvent, the support, or the active site of the enzyme. Immobilization represents a promising and straightforward route to obtaining high activity and stability of enzymes. Along with physicochemical methods of enzyme stabilization, such as additive approach, chemical modification, also protein engineering and high-throughput screening can be used to enhance the performance of biocatalysts. It is quite important to obtain mutant libraries designed according to a “small but smart” concept.

This Special Issue aims to contribute to the current knowledge in the field of biocatalysis, e.g., in pharmacy, food industry and environmental application. Articles focusing on the improvement of the efficiency of biocatalysts and enzymatic processes, bioinformatics, and protein engineering are welcomed. In this Special Issue, we invite the submission of original research articles and reviews.

We look forward to your contributions.

Prof. Dr. Maciej Szaleniec
Dr. Marek Adamczak
Dr. Bartosz Brzozowski
Guest Editors

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Keywords

  • biocatalysis
  • biotransformation
  • enzyme modification
  • protein engineering
  • medium engineering
  • non-conventional media
  • enzyme immobilization
  • directed evolution

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Published Papers (1 paper)

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Research

11 pages, 6005 KiB  
Article
Characterization of a PBAT Degradation Carboxylesterase from Thermobacillus composti KWC4
by Pan Wu, Zhishuai Li, Jian Gao, Yipei Zhao, Hao Wang, Huimin Qin, Qun Gu, Ren Wei, Weidong Liu and Xu Han
Catalysts 2023, 13(2), 340; https://doi.org/10.3390/catal13020340 - 3 Feb 2023
Cited by 10 | Viewed by 2685
Abstract
The large amount of waste synthetic polyester plastics has complicated waste management and also endangering the environment due to improper littering. In this study, a novel carboxylesterase from Thermobacillus composti KWC4 (Tcca) was identified, heterologously expressed in Escherichia coli, purified and characterized with [...] Read more.
The large amount of waste synthetic polyester plastics has complicated waste management and also endangering the environment due to improper littering. In this study, a novel carboxylesterase from Thermobacillus composti KWC4 (Tcca) was identified, heterologously expressed in Escherichia coli, purified and characterized with various plastic substrates. Irregular grooves were detected on polybutylene adipate terephthalate (PBAT) film by scanning electron microscopy (SEM) after Tcca treatment, and Tcca can also hydrolyze short–chain diester bis(hydroxyethyl) terephthalate (BHET). The optimal pH and temperature for Tcca were 7.0 and 40 °C, respectively. In order to explore its catalytic mechanism and improve its potential for plastic hydrolysis, we modeled the protein structure of Tcca and compared it with its homologous structures, and we identified positions that might be crucial for the binding of substrates. We generated a variety of Tcca variants by mutating these key positions; the variant F325A exhibited a more than 1.4–fold improvement in PBAT hydrolytic activity, and E80A exhibited a more than 4.1–fold increase in BHET activity when compared to the wild type. Tcca and its variants demonstrated future applicability for the recycling of bioplastic waste containing a PBAT fraction. Full article
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