Special Issue "Biocatalytic Applications in Biotechnology"

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

Deadline for manuscript submissions: 31 January 2020.

Special Issue Editors

Guest Editor
Prof. Dr. Emmanuel M. Papamichael Website E-Mail
Enzyme Biotechnology and Genetic Engineering Group, Department of Chemistry, University of Ioannina, Ioannina 45110, Greece
Interests: chemical and enzyme kinetics (homogeneous/heterogeneous reactions); enzymology; enzyme biotechnology; biofuel production; statistical analysis of experimental data; experimental design; computer programming
Guest Editor
Dr. Panagiota-Yiolanda Stergiou E-Mail
Enzyme Biotechnology and Genetic Engineering Group, Department of Chemistry, University of Ioannina, Ioannina 45110, Greece
Interests: biocatalysis; enzyme biotechnology (food biotechnology and biofuel production); experimental design

Special Issue Information

Dear Colleagues,

Nowadays, the vast increasing demand of novel biotechnological products is supported through the continuous development of biocatalytic applications. As a consequence, the progress of research regarding the enzymatic catalysis in aqueous, non-aqueous, organic (polar or non-polar), and/or non-solvent media is decisive. Experimental design methods, which also may comprise of in silico studies; the design of specific reactors and conditions; reactions of significant chemical and/or biochemical processes, which are relevant to industrial production; enzyme kinetic methods; the investigation of enzymatic mechanisms; and the use of immobilized enzymes and/or microbial cells on various inert matrices are importantly useful. A plethora of enzymes of several classes, which may potentially be used as biocatalysts in biotechnological applications, are available today. Among these enzymes, the more common are oxidoreductases (e.g., laccase, catalase, glucose oxidase, etc.), hydrolases (e.g., amylases, lipases, proteases, amidases, cellulases, esterases, etc.), isopmerases (e.g., epimerases, topoisomerases, mutases, etc.), and others. By means of the aforementioned biocatalysts and the utilization of specific biotechnological methods, important, cost-effective, sustainable, and environmentally friendly processes have been applied for the synthesis and/or the conversion of a huge amount of market-required products.

Prof. Dr. Emmanuel M. Papamichael
Dr. Panagiota-Yiolanda Stergiou
Guest Editors

Manuscript Submission Information

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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 1600 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

  • Enzymatic catalysis
  • Biocatalysis
  • Biotechnological applications
  • In silico simulations
  • Experimental design
  • Reactor design
  • Process optimization
  • Immobilized enzymes
  • Whole cell biocatalysis

Published Papers (4 papers)

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Research

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Open AccessArticle
Catalytic Activities of Multimeric G-Quadruplex DNAzymes
Catalysts 2019, 9(7), 613; https://doi.org/10.3390/catal9070613 - 19 Jul 2019
Abstract
G-quadruplex DNAzymes are short DNA aptamers with repeating G4 quartets bound in a non-covalent complex with hemin. These G4/Hemin structures exhibit versatile peroxidase-like catalytic activity with a wide range of potential applications in biosensing and biotechnology. Current efforts are aimed at gaining a [...] Read more.
G-quadruplex DNAzymes are short DNA aptamers with repeating G4 quartets bound in a non-covalent complex with hemin. These G4/Hemin structures exhibit versatile peroxidase-like catalytic activity with a wide range of potential applications in biosensing and biotechnology. Current efforts are aimed at gaining a better understanding of the molecular mechanism of DNAzyme catalysis as well as devising strategies for improving their catalytic efficiency. Multimerisation of discrete units of G-quadruplexes to form multivalent DNAzyes is an emerging design strategy aimed at enhancing the peroxidase activities of DNAzymes. While this approach holds promise of generating more active multivalent G-quadruplex DNAzymes, few examples have been studied and it is not clear what factors determine the enhancement of catalytic activities of multimeric DNAzymes. In this study, we report the design and characterisation of multimers of five G-quadruplex sequences (AS1411, Bcl-2, c-MYC, PS5.M and PS2.M). Our results show that multimerisation of G-quadruplexes that form parallel structure (AS1411, Bcl-2, c-MYC) leads to significant rate enhancements characteristic of cooperative and/or synergistic interactions between the monomeric units. In contrast, multimerisation of DNA sequences that form non-parallel structures (PS5.M and PS2.M) did not exhibit similar levels of synergistic increase in activities. These results show that design of multivalent G4/Hemin structures could lead to a new set of versatile and efficient DNAzymes with enhanced capacity to catalyse peroxidase-mimic reactions. Full article
(This article belongs to the Special Issue Biocatalytic Applications in Biotechnology)
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Open AccessArticle
Biotransformation with a New Acinetobacter sp. Isolate for Highly Enantioselective Synthesis of a Chiral Intermediate of Miconazole
Catalysts 2019, 9(5), 462; https://doi.org/10.3390/catal9050462 - 20 May 2019
Abstract
(R)-2-Chloro-1-(2,4-dichlorophenyl) ethanol is a chiral intermediate of the antifungal agent Miconazole. A bacterial strain, ZJPH1806, capable of the biocatalysis of 2-chloro-1-(2,4-dichlorophenyl) ethanone, to (R)-2-chloro-1-(2,4-dichlorophenyl) ethanol with highly stereoselectivity was isolated from a soil sample. It was identified as the [...] Read more.
(R)-2-Chloro-1-(2,4-dichlorophenyl) ethanol is a chiral intermediate of the antifungal agent Miconazole. A bacterial strain, ZJPH1806, capable of the biocatalysis of 2-chloro-1-(2,4-dichlorophenyl) ethanone, to (R)-2-chloro-1-(2,4-dichlorophenyl) ethanol with highly stereoselectivity was isolated from a soil sample. It was identified as the Acinetobacter sp., according to its morphological observation, physiological-biochemical identification, and 16S rDNA sequence analysis. After optimizing the key reaction conditions, it was demonstrated that the bioreduction of 2-chloro-1-(2,4-dichlorophenyl) ethanone was effectively transformed at relatively high conversion temperatures, along with glycerol as cosubstrate in coenzyme regeneration. The asymmetric reduction of the substrate had reached 83.2% yield with an enantiomeric excess (ee) of greater than 99.9% at 2 g/L of 2-chloro-1-(2,4-dichlorophenyl) ethanone; the reaction was conducted at 40 °C for 26 h using resting cells of the Acinetobacter sp. ZJPH1806 as the biocatalyst. The yield had increased by nearly 2.9-fold (from 28.6% to 83.2%). In the present study, a simple and novel whole-cell-mediated biocatalytic route was applied for the highly enantioselective synthesis of (R)-2-chloro-1-(2,4-dichlorophenyl) ethanol, which allowed the production of a valuable chiral intermediate method to be transformed into a versatile tool for drug synthesis. Full article
(This article belongs to the Special Issue Biocatalytic Applications in Biotechnology)
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Open AccessArticle
Enhancing Enzymatic Properties of Endoglucanase I Enzyme from Trichoderma Reesei via Swapping from Cellobiohydrolase I Enzyme
Catalysts 2019, 9(2), 130; https://doi.org/10.3390/catal9020130 - 01 Feb 2019
Cited by 1
Abstract
Utilizing plant-based materials as a biofuel source is an increasingly popular attempt to redesign the global energy cycle. This endeavour underlines the potential of cellulase enzymes for green energy production and requires the structural and functional engineering of natural enzymes to enhance their [...] Read more.
Utilizing plant-based materials as a biofuel source is an increasingly popular attempt to redesign the global energy cycle. This endeavour underlines the potential of cellulase enzymes for green energy production and requires the structural and functional engineering of natural enzymes to enhance their utilization. In this work, we aimed to engineer enzymatic and functional properties of Endoglucanase I (EGI) by swapping the Ala43-Gly83 region of Cellobiohydrolase I (CBHI) from Trichoderma reesei. Herein, we report the enhanced enzymatic activity and improved thermal stability of the engineered enzyme, called EGI_swapped, compared to EGI. The difference in the enzymatic activity profile of EGI_swapped and the EGI enzymes became more pronounced upon increasing metal-ion concentrations in the reaction media. Notably, the engineered enzyme retained a considerable level of enzymatic activity after thermal incubation for 90 min at 70 °C while EGI completely lost its enzymatic activity. Circular Dichroism spectroscopy studies revealed distinctive conformational and thermal susceptibility differences between EGI_swapped and EGI enzymes, confirming the improved structural integrity of the swapped enzyme. This study highlights the importance of swapping the metal-ion coordination region in the engineering of EGI enzyme for enhanced structural and thermal stability. Full article
(This article belongs to the Special Issue Biocatalytic Applications in Biotechnology)
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Review

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Open AccessReview
Microbial Phosphotriesterase: Structure, Function, and Biotechnological Applications
Catalysts 2019, 9(8), 671; https://doi.org/10.3390/catal9080671 - 07 Aug 2019
Abstract
The role of phosphotriesterase as an enzyme which is able to hydrolyze organophosphate compounds cannot be disputed. Contamination by organophosphate (OP) compounds in the environment is alarming, and even more worrying is the toxicity of this compound, which affects the nervous system. Thus, [...] Read more.
The role of phosphotriesterase as an enzyme which is able to hydrolyze organophosphate compounds cannot be disputed. Contamination by organophosphate (OP) compounds in the environment is alarming, and even more worrying is the toxicity of this compound, which affects the nervous system. Thus, it is important to find a safer way to detoxify, detect and recuperate from the toxicity effects of this compound. Phosphotriesterases (PTEs) are mostly isolated from soil bacteria and are classified as metalloenzymes or metal-dependent enzymes that contain bimetals at the active site. There are three separate pockets to accommodate the substrate into the active site of each PTE. This enzyme generally shows a high catalytic activity towards phosphotriesters. These microbial enzymes are robust and easy to manipulate. Currently, PTEs are widely studied for the detection, detoxification, and enzyme therapies for OP compound poisoning incidents. The discovery and understanding of PTEs would pave ways for greener approaches in biotechnological applications and to solve environmental issues relating to OP contamination. Full article
(This article belongs to the Special Issue Biocatalytic Applications in Biotechnology)
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