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Enzyme Catalysis: Advances, Techniques, and Outlooks
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Enzyme Catalysis: Advances, Techniques, and Outlooks

A special issue of Applied Sciences (ISSN 2076-3417). This special issue belongs to the section "Applied Biosciences and Bioengineering".

Deadline for manuscript submissions: closed (15 April 2022) | Viewed by 31474

Printed Edition Available!
A printed edition of this Special Issue is available here.

Special Issue Editor

Dr. In Jung Kim

E-Mail Website
Guest Editor
College of Agriculture and Life Science, Kyungpook National University, Daegu 41566, Republic of Korea
Interests: biocatalysis; enzyme kinetics; protein engineering; biochemical assay
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Enzyme catalysis can be applied in a variety of industrial fields, such as biorefinery, biochemicals, foods, pharmaceuticals, etc. As a greener and more selective process, enzyme catalysis is a powerful tool as an alternative to chemical catalysis for the sustainable production of desired compounds. The basic requirements for enzymes to be used as catalysts in industrial applications are high catalytic efficiency, high thermostability, and desired substrate scope. As represented by Frances Arnold’s win of the Nobel prize in 2018, protein engineering technology is making scaled-up industrial applications of enzymes even more real.

This Special Issue covers comprehensive topics and technologies on industrial enzymes and aims to contribute to the development of relevant fields. We warmly invite your submissions to this Special Issue on “Enzyme Catalysis: Advances, Techniques, and Outlooks” to explore recent advances and technologies in the field of enzyme catalysis.

Dr. In Jung Kim
Guest Editor

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. Applied Sciences is an international peer-reviewed open access semimonthly 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 2400 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

  • Enzyme catalysis
  • Biocatalysis
  • Protein engineering
  • Enzyme kinetics
  • Biochemical analysis
  • Industrial enzyme

Published Papers (7 papers)

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Editorial

Jump to: Research, Review

3 pages, 170 KiB  
Editorial
Enzyme Catalysis: Advances, Techniques, and Outlooks
by In Jung Kim
Appl. Sci. 2022, 12(16), 8036; https://0-doi-org.brum.beds.ac.uk/10.3390/app12168036 - 11 Aug 2022
Cited by 1 | Viewed by 1190
Abstract
Biocatalysis using enzymes is a powerful strategy that can be employed in a variety of industries for the production of biofuel, biochemicals, pharmaceuticals, and foods, etc [...] Full article
(This article belongs to the Special Issue Enzyme Catalysis: Advances, Techniques, and Outlooks)

Research

Jump to: Editorial, Review

11 pages, 3136 KiB  
Article
Crystal Structure of Human Lysozyme Complexed with N-Acetyl-α-d-glucosamine
by Ki Hyun Nam
Appl. Sci. 2022, 12(9), 4363; https://0-doi-org.brum.beds.ac.uk/10.3390/app12094363 - 26 Apr 2022
Cited by 5 | Viewed by 3447
Abstract
Human lysozyme is a natural non-specific immune protein that participates in the immune response of infants against bacterial and viral infections. Lysozyme is a well-known hydrolase that cleaves peptidoglycan in bacterial cell walls. Several crystal structures of human lysozyme have been reported, but [...] Read more.
Human lysozyme is a natural non-specific immune protein that participates in the immune response of infants against bacterial and viral infections. Lysozyme is a well-known hydrolase that cleaves peptidoglycan in bacterial cell walls. Several crystal structures of human lysozyme have been reported, but little is known regarding how it recognizes sugar molecules. In this study, the crystal structures of human lysozyme in its native and two N-acetyl-α-d-glucosamine (α-D-NAG)-bound forms were determined at 1.3 Å and 1.55/1.60 Å resolution, respectively. Human lysozyme formed a typical c-type lysozyme fold and the α-D-NAG molecule was bound to the middle of subsites C and D. The N-acetyl and glucosamine groups of α-D-NAG were stabilized by hydrophobic interactions (Val117, Ala126, and Trp127), hydrogen bonds (Asn64, Asn78, Ala126, and Val128), and water bridges. Conformational changes of Arg80, Tyr81, Val128, and Arg131 of human lysozyme were observed due to the interactions of α-D-NAG with the active-site cleft. The binding configuration of α-D-NAG in human lysozyme was distinct compared with that of other sugar-bound lysozymes. Findings from this structural analysis provide a better understanding of the sugar recognition of human lysozyme during the immune response to microbial pathogens. Full article
(This article belongs to the Special Issue Enzyme Catalysis: Advances, Techniques, and Outlooks)
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12 pages, 2331 KiB  
Article
l-Fucose Synthesis Using a Halo- and Thermophilic l-Fucose Isomerase from Polyextremophilic Halothermothrix orenii
by In Jung Kim and Kyoung Heon Kim
Appl. Sci. 2022, 12(8), 4029; https://0-doi-org.brum.beds.ac.uk/10.3390/app12084029 - 15 Apr 2022
Cited by 5 | Viewed by 1718
Abstract
l-Fucose isomerase (l-FucI)-mediated isomerization is a promising biotechnological approach for synthesizing various rare sugars of industrial significance, including l-fucose. Extremozymes that can retain their functional conformation under extreme conditions, such as high temperature and salinity, offer favorable applications in [...] Read more.
l-Fucose isomerase (l-FucI)-mediated isomerization is a promising biotechnological approach for synthesizing various rare sugars of industrial significance, including l-fucose. Extremozymes that can retain their functional conformation under extreme conditions, such as high temperature and salinity, offer favorable applications in bioprocesses that accompany harsh conditions. To date, only one thermophilic l-FucI has been characterized for l-fucose synthesis. Here, we report l-FucI from Halothermothrix orenii (HoFucI) which exhibits both halophilic and thermophilic properties. When evaluated under various biochemical conditions, HoFucI exhibited optimal activities at 50–60 °C and pH 7 with 0.5–1 M NaCl in the presence of 1 mM Mn2+ as a cofactor. The results obtained here show a unique feature of HoFucI as a polyextremozyme, which facilitates the biotechnological production of l-fucose using this enzyme. Full article
(This article belongs to the Special Issue Enzyme Catalysis: Advances, Techniques, and Outlooks)
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15 pages, 3913 KiB  
Article
Compatibility and Washing Performance of Compound Protease Detergent
by Wei Zhang, Jintao Wu, Jing Xiao, Mingyao Zhu and Haichuan Yang
Appl. Sci. 2022, 12(1), 150; https://0-doi-org.brum.beds.ac.uk/10.3390/app12010150 - 24 Dec 2021
Cited by 5 | Viewed by 4298
Abstract
Protease is the main enzyme of detergent. Through the combination of different proteases and the combination of protease and detergent additives, it can adapt to different washing conditions to improve the washing effect. In this experiment, whiteness determination, microscope scanning, Fourier transform infrared [...] Read more.
Protease is the main enzyme of detergent. Through the combination of different proteases and the combination of protease and detergent additives, it can adapt to different washing conditions to improve the washing effect. In this experiment, whiteness determination, microscope scanning, Fourier transform infrared spectroscopy, and X-ray photoelectron spectroscopy were used to detect the whiteness values of the cloth pieces before and after washing, as well as the stain residue between the fibers on the surface of the cloth pieces. The protease detergent formula with better decontamination and anti-deposition effects was selected. The combination of alkaline protease, keratinase, and trypsin was cost-effective in removing stains. Polyacrylamide gel electrophoresis showed that the molecular weight of the protein significantly changed after adding the enzyme preparation during washing, and the molecular weight of the protein was directly proportional to protein redeposition. The composite protease had a better comprehensive decontamination effect, and when compatible with suitable surfactants, anti-redeposition agents, and water-softening agents, the compound protease detergent exhibited a stronger decontamination ability than commercial detergents. Full article
(This article belongs to the Special Issue Enzyme Catalysis: Advances, Techniques, and Outlooks)
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8 pages, 1279 KiB  
Article
Kinetic Analysis Misinterpretations Due to the Occurrence of Enzyme Inhibition by Reaction Product: Comparison between Initial Velocities and Reaction Time Course Methodologies
by Joana M. C. Fernandes, Albino A. Dias and Rui M. F. Bezerra
Appl. Sci. 2022, 12(1), 102; https://0-doi-org.brum.beds.ac.uk/10.3390/app12010102 - 23 Dec 2021
Cited by 1 | Viewed by 1994
Abstract
The Michaelis–Menten equation (MME) has been extensively used in biochemical reactions, but it is not appropriate when the reaction product inhibits the enzyme. Under these circumstances, each determined initial velocity, v0, is one experimental point that actually belongs to a different [...] Read more.
The Michaelis–Menten equation (MME) has been extensively used in biochemical reactions, but it is not appropriate when the reaction product inhibits the enzyme. Under these circumstances, each determined initial velocity, v0, is one experimental point that actually belongs to a different MME because enzymatic product inhibition occurs as the reaction starts. Furthermore, the inhibition effect is not constant, since the concentration of the product inhibitor rises as time increases. To unveil the hidden enzyme inhibition and to simultaneously demonstrate the superiority of an integrated Michaelis–Menten equation (IMME), the same range of data points, assuming product inhibition and the presence of a second different inhibitor, was used for kinetic analysis with both methodologies. This study highlights the superiority of the IMME methodology for when the enzyme is inhibited by the reaction product, giving a more coherent inhibition model and more accurate kinetic constants than the classical MME methodology. Full article
(This article belongs to the Special Issue Enzyme Catalysis: Advances, Techniques, and Outlooks)
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13 pages, 3057 KiB  
Article
Production of a Human Metabolite of Atorvastatin by Bacterial CYP102A1 Peroxygenase
by Thi Huong Ha Nguyen, Soo-Jin Yeom and Chul-Ho Yun
Appl. Sci. 2021, 11(2), 603; https://0-doi-org.brum.beds.ac.uk/10.3390/app11020603 - 10 Jan 2021
Cited by 13 | Viewed by 2542
Abstract
Atorvastatin is a widely used statin drug that prevents cardiovascular disease and treats hyperlipidemia. The major metabolites in humans are 2-OH and 4-OH atorvastatin, which are active metabolites known to show highly inhibiting effects on 3-hydroxy-3-methylglutaryl-CoA reductase activity. Producing the hydroxylated metabolites by [...] Read more.
Atorvastatin is a widely used statin drug that prevents cardiovascular disease and treats hyperlipidemia. The major metabolites in humans are 2-OH and 4-OH atorvastatin, which are active metabolites known to show highly inhibiting effects on 3-hydroxy-3-methylglutaryl-CoA reductase activity. Producing the hydroxylated metabolites by biocatalysts using enzymes and whole-cell biotransformation is more desirable than chemical synthesis. It is more eco-friendly and can increase the yield of desired products. In this study, we have found an enzymatic strategy of P450 enzymes for highly efficient synthesis of the 4-OH atorvastatin, which is an expensive commercial product, by using bacterial CYP102A1 peroxygenase activity with hydrogen peroxide without NADPH. We obtained a set of CYP102A1 mutants with high catalytic activity toward atorvastatin using enzyme library generation, high-throughput screening of highly active mutants, and enzymatic characterization of the mutants. In the hydrogen peroxide supported reactions, a mutant, with nine changed amino acid residues compared to a wild-type among tested mutants, showed the highest catalytic activity of atorvastatin 4-hydroxylation (1.8 min−1). This result shows that CYP102A1 can catalyze atorvastatin 4-hydroxylation by peroxide-dependent oxidation with high catalytic activity. The advantages of CYP102A1 peroxygenase activity over NADPH-supported monooxygenase activity are discussed. Taken together, we suggest that the P450 peroxygenase activity can be used to produce drugs’ metabolites for further studies of their efficacy and safety. Full article
(This article belongs to the Special Issue Enzyme Catalysis: Advances, Techniques, and Outlooks)
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Review

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12 pages, 2880 KiB  
Review
Glucose Isomerase: Functions, Structures, and Applications
by Ki Hyun Nam
Appl. Sci. 2022, 12(1), 428; https://0-doi-org.brum.beds.ac.uk/10.3390/app12010428 - 03 Jan 2022
Cited by 22 | Viewed by 14815
Abstract
Glucose isomerase (GI, also known as xylose isomerase) reversibly isomerizes D-glucose and D-xylose to D-fructose and D-xylulose, respectively. GI plays an important role in sugar metabolism, fulfilling nutritional requirements in bacteria. In addition, GI is an important industrial enzyme for the production of [...] Read more.
Glucose isomerase (GI, also known as xylose isomerase) reversibly isomerizes D-glucose and D-xylose to D-fructose and D-xylulose, respectively. GI plays an important role in sugar metabolism, fulfilling nutritional requirements in bacteria. In addition, GI is an important industrial enzyme for the production of high-fructose corn syrup and bioethanol. This review introduces the functions, structure, and applications of GI, in addition to presenting updated information on the characteristics of newly discovered GIs and structural information regarding the metal-binding active site of GI and its interaction with the inhibitor xylitol. This review provides an overview of recent advancements in the characterization and engineering of GI, as well as its industrial applications, and will help to guide future research in this field. Full article
(This article belongs to the Special Issue Enzyme Catalysis: Advances, Techniques, and Outlooks)
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