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Catalysts
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Recent Advances in Enzyme Technology
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Recent Advances in Enzyme Technology

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

Deadline for manuscript submissions: closed (31 August 2021) | Viewed by 14450

Special Issue Editors

Dr. Peter Adewale

E-Mail Website
Guest Editor
Bioprocessing and BioCatalysis, National Research Council Canada, K1N 5A2, Ottawa, Canada
Interests: biocatalysis; biomaterials; biofuels; bioprocessing; process optimization; reaction kinetics
Special Issues, Collections and Topics in MDPI journals
Dr. Michele C. Loewen

E-Mail Website
Guest Editor
National Research Council of Canada, Aquatic and Crop Resources Development Research Center, Ottawa K1A 0R6, Canada
Interests: abscisic acid biosynthesis; abscisic acid perception; abscisic acid signal transduction; phytohormone crosstalk; cereal pathogens; fungal biocontrol
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Chemical catalysis has been widely adopted for industrial applications due to its high throughput rates and short production time. However, this process has several inherent limitations related to high energy consumption and severe environmental impacts, such as wastewater treatment, expensive products and catalysts recovery, etc. The application of biocatalytic technology has gained immense attention in the chemical and bioindustry due to its sustainable mild reaction conditions. These include low reaction temperature conditions, substrate specificity, recyclability, more natural product separation and recovery, and elimination of wastewater treatment costs. In order to reduce enzyme costs, the catalytic effectiveness and chemo-, regio-, and stereoselectivity of an enzyme can be enhanced and modified using protein engineering. The state-of-the-art includes directed evolution, genetic code expansion, strain improvement, the use of high throughput productive recombinant strains, immobilization, and discovery of new enzymes. The modification of amino acid sequences that are found in nature leads to improved proteins with unique functionalities, such as resistance to the harsh reaction conditions, high activity, and thermostability. Assisted intensification techniques have gained incredible attention in recent years for enzyme reaction enhancement. The application of intensification techniques such as ultrasonication, microwave, and pulsed electric field has shown a significant reduction in enzyme reaction time, with relevance to lowering bioprocessing costs. 

This Special Issue aims to contribute to recent advances in enzyme technology for the biomanufacturing of chemicals, biomaterials, biofuels, and pharmaceuticals. High-quality original research papers and review articles on the development of new approaches to improve catalytic efficiency of enzymes, biocatalytic process intensification, enzyme immobilization, biocatalytic kinetics and optimization, green chemistry and their applications in the biosynthesis of chemicals, biofuels, pilot, and large-scale developments of various bioproducts are welcome.

Dr. Peter Adewale
Dr. Michele C. Loewen
Guest Editors

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 100 words) can be sent to the Editorial Office for announcement on this website.

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 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

  • Biocatalytic process intensification
  • Biocatalytic reaction
  • Enzyme engineering
  • Immobilization
  • Metabolic engineering
  • Green chemistry
  • Genetic code expansion
  • Enzyme kinetics and optimization
  • Biomass
  • Industrial biotechnology

Published Papers (4 papers)

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Research

18 pages, 3656 KiB  
Article
CalkGH9T: A Glycoside Hydrolase Family 9 Enzyme from Clostridium alkalicellulosi
by Paripok Phitsuwan, Sengthong Lee, Techly San and Khanok Ratanakhanokchai
Catalysts 2021, 11(8), 1011; https://doi.org/10.3390/catal11081011 - 22 Aug 2021
Cited by 4 | Viewed by 2708
Abstract
Glycoside hydrolase family 9 (GH9) endoglucanases are important enzymes for cellulose degradation. However, their activity on cellulose is diverse. Here, we cloned and expressed one GH9 enzyme (CalkGH9T) from Clostridium alkalicellulosi in Escherichia coli. CalkGH9T has a modular structure, [...] Read more.
Glycoside hydrolase family 9 (GH9) endoglucanases are important enzymes for cellulose degradation. However, their activity on cellulose is diverse. Here, we cloned and expressed one GH9 enzyme (CalkGH9T) from Clostridium alkalicellulosi in Escherichia coli. CalkGH9T has a modular structure, containing one GH9 catalytic module, two family 3 carbohydrate binding modules, and one type I dockerin domain. CalkGH9T exhibited maximal activity at pH 7.0–8.0 and 55 °C and was resistant to urea and NaCl. It efficiently hydrolyzed carboxymethyl cellulose (CMC) but poorly degraded regenerated amorphous cellulose (RAC). Despite strongly binding to Avicel, CalkGH9T lacked the ability to hydrolyze this substrate. The hydrolysis of CMC by CalkGH9T produced a series of cello-oligomers, with cellotetraose being preferentially released. Similar proportions of soluble and insoluble reducing ends generated by hydrolysis of RAC indicated non-processive activity. Our study extends our knowledge of the molecular mechanism of cellulose hydrolysis by GH9 family endoglucanases with industrial relevance. Full article
(This article belongs to the Special Issue Recent Advances in Enzyme Technology)
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9 pages, 1751 KiB  
Communication
Production of Ethylene Glycol from Glycerol Using an In Vitro Enzymatic Cascade
by Kai Li, Weikang Sun, Wensi Meng, Jinxin Yan, Yipeng Zhang, Shiting Guo, Chuanjuan Lü, Cuiqing Ma and Chao Gao
Catalysts 2021, 11(2), 214; https://doi.org/10.3390/catal11020214 - 05 Feb 2021
Cited by 8 | Viewed by 5716
Abstract
Glycerol is a readily available and inexpensive substance that is mostly generated during biofuel production processes. In order to ensure the viability of the biofuel industry, it is essential to develop complementing technologies for the resource utilization of glycerol. Ethylene glycol is a [...] Read more.
Glycerol is a readily available and inexpensive substance that is mostly generated during biofuel production processes. In order to ensure the viability of the biofuel industry, it is essential to develop complementing technologies for the resource utilization of glycerol. Ethylene glycol is a two-carbon organic chemical with multiple applications and a huge market. In this study, an artificial enzymatic cascade comprised alditol oxidase, catalase, glyoxylate/hydroxypyruvate reductase, pyruvate decarboxylase and lactaldehyde:propanediol oxidoreductase was developed for the production of ethylene glycol from glycerol. The reduced nicotinamide adenine dinucleotide (NADH) generated during the dehydrogenation of the glycerol oxidation product d-glycerate can be as the reductant to support the ethylene glycol production. Using this in vitro synthetic system with self-sufficient NADH recycling, 7.64 ± 0.15 mM ethylene glycol was produced from 10 mM glycerol in 10 h, with a high yield of 0.515 ± 0.1 g/g. The in vitro enzymatic cascade is not only a promising alternative for the generation of ethylene glycol but also a successful example of the value-added utilization of glycerol. Full article
(This article belongs to the Special Issue Recent Advances in Enzyme Technology)
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15 pages, 2545 KiB  
Article
Modulation of Human Mesenchymal Stem Cells by Electrical Stimulation Using an Enzymatic Biofuel Cell
by Won-Yong Jeon, Seyoung Mun, Wei Beng Ng, Keunsoo Kang, Kyudong Han, Sohyun Hwang, Hyug-Han Kim and Jae Ho Lee
Catalysts 2021, 11(1), 62; https://doi.org/10.3390/catal11010062 - 05 Jan 2021
Cited by 1 | Viewed by 2369
Abstract
Enzymatic biofuel cells (EBFCs) have excellent potential as components in bioelectronic devices, especially as active biointerfaces to regulate stem cell behavior for regenerative medicine applications. However, it remains unclear to what extent EBFC-generated electrical stimulation can regulate the functional behavior of human adipose-derived [...] Read more.
Enzymatic biofuel cells (EBFCs) have excellent potential as components in bioelectronic devices, especially as active biointerfaces to regulate stem cell behavior for regenerative medicine applications. However, it remains unclear to what extent EBFC-generated electrical stimulation can regulate the functional behavior of human adipose-derived mesenchymal stem cells (hAD-MSCs) at the morphological and gene expression levels. Herein, we investigated the effect of EBFC-generated electrical stimulation on hAD-MSC cell morphology and gene expression using next-generation RNA sequencing. We tested three different electrical currents, 127 ± 9, 248 ± 15, and 598 ± 75 nA/cm2, in mesenchymal stem cells. We performed transcriptome profiling to analyze the impact of EBFC-derived electrical current on gene expression using next generation sequencing (NGS). We also observed changes in cytoskeleton arrangement and analyzed gene expression that depends on the electrical stimulation. The electrical stimulation of EBFC changes cell morphology through cytoskeleton re-arrangement. In particular, the results of whole transcriptome NGS showed that specific gene clusters were up- or down-regulated depending on the magnitude of applied electrical current of EBFC. In conclusion, this study demonstrates that EBFC-generated electrical stimulation can influence the morphological and gene expression properties of stem cells; such capabilities can be useful for regenerative medicine applications such as bioelectronic devices. Full article
(This article belongs to the Special Issue Recent Advances in Enzyme Technology)
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14 pages, 1164 KiB  
Article
Amino Acid Replacement at Position 228 Induces Fluctuation in the Ω-Loop of KPC-3 and Reduces the Affinity against Oxyimino Cephalosporins: Kinetic and Molecular Dynamics Studies
by Alessandra Piccirilli, Fabrizia Brisdelli, Jean Denis Docquier, Massimiliano Aschi, Sabrina Cherubini, Filomena De Luca, André Matagne, Gianfranco Amicosante and Mariagrazia Perilli
Catalysts 2020, 10(12), 1474; https://doi.org/10.3390/catal10121474 - 16 Dec 2020
Cited by 2 | Viewed by 1564
Abstract
KPC enzymes are the most common class A carbapenemases globally diffused. The peculiarity of this family of β-lactamases is represented by their ability to hydrolyse all classes of β-lactams, including carbapenems, posing a serious problem to public health. In the present study, seven [...] Read more.
KPC enzymes are the most common class A carbapenemases globally diffused. The peculiarity of this family of β-lactamases is represented by their ability to hydrolyse all classes of β-lactams, including carbapenems, posing a serious problem to public health. In the present study, seven laboratory mutants of KPC-3 (D228S, D228W, D228M, D228K, D228L, D228I and D228G) were generated by site-saturation mutagenesis to explore the role of residue 228, a non-active site residue. Compared to KPC-3, the seven mutants showed evident differences in kcat and Km values calculated for some penicillins, cephalosporins and carbapenems. In particular, D228S and D228M showed a significant increase of Km values for cefotaxime and ceftazidime. Circular dichroism (CD) experiments have demonstrated that substitution at position 228 does not affect the secondary structure of the mutants. Molecular dynamics (MD) simulations were performed on KPC-3, D228S and D228M uncomplexed and complexed with cefotaxime (substrate). Although the residue 228 is located far from the active site, between α11 helix and β7 sheet in the opposite site of the Ω-loop, amino acid substitution at this position generates mechanical effects in the active site resulting in enzyme activity changes. Full article
(This article belongs to the Special Issue Recent Advances in Enzyme Technology)
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