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Catalysts
Special Issues
Enzyme and Biocatalysis Application
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Enzyme and Biocatalysis Application

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

Deadline for manuscript submissions: 30 November 2024 | Viewed by 1248

Special Issue Editors

Prof. Dr. Chia-Hung Kuo

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Guest Editor
Department of Seafood Science, National Kaohsiung University of Science and Technology, Kaohsiung 81157, Taiwan
Interests: food analysis; food processing; cellulase; lipase esterification and trans esterification; amylase; enzymatic kinetics; ultrasound-assisted enzymatic reaction; enzyme extraction; biotransformation; saccharification; response surface methodology; artificial neural network; wine fermentation
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Chwen-Jen Shieh

E-Mail Website
Guest Editor
Biotechnology Center, National Chung-Hsing University, Taichung, Taiwan
Interests: biodiesel; lipid biocatalysis; enzyme technology; bioprocess optimization; supercritical fluid technology; Chinese herb medicine biotechnology
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Yung-Chuan Liu

E-Mail Website
Guest Editor
Department of Chemical Engineering, National Chung Hsing University, Taichung 402, Taiwan
Interests: fermentation technology; protein engineering; immunoassay; membrane technology; molecular engineering
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Enzymes, with their remarkable specificity, catalyze key reactions essential for various processes that are widely used for pharmaceuticals, biochemical synthesis, agriculture science, food science and environmental remediation. The Special Issue on Enzyme and Biocatalysis Application aims to showcase the latest advancements, methodologies, and applications of enzyme and biocatalysis. It welcomes contributions that explore various aspects of enzyme application, as well as innovative biocatalytic processes in the fields of pharmaceuticals, biochemical synthesis, biotechnology, food science, and environmental remediation. This includes enzyme production, biocatalytic process development, enzymatic synthesis, biotransformation, enzyme engineering and enzyme immobilization. In this Special Issue, we welcome original research articles and reviews focused on all aspects of enzymes applications, such as biocatalysis, process optimization, ultrasonic process, fine chemical production, enzymatic-assisted extraction, enzyme production, biocatalytic processes, environmental protection, bio-reactors, food processes, biomass utilization, bioresource application, bio-transformations, enzymology, biological activity, enzymatic synthesis of value-added chemicals, nanotechnology; environment and biodiversity; and bioremediation and so on. Overall, it aims to highlight the significance of enzymes and biocatalysis in addressing global challenges and advancing sustainable solutions.

Prof. Dr. Chia-Hung Kuo
Prof. Dr. Chwen-Jen Shieh
Prof. Dr. Yung-Chuan Liu
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 2200 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 production
  • enzyme purification
  • biocatalysis
  • optimization
  • lipase
  • cellulase
  • protease
  • amylase
  • biofuels
  • enzymatic-catalyzed synthesis
  • enzyme immobilization
  • biomass utilization
  • environmental protection
  • glucosidase
  • biotransformation
  • enzymatic kinetics
  • ultrasound-assisted enzymatic reaction
  • bio-reactor
  • enzymatic-assisted extraction
  • experimental design
  • response surface methodology (RSM)

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Further information on MDPI's Special Issue polices can be found here.

Published Papers (2 papers)

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Research

17 pages, 4541 KiB  
Article
Identification of Five Robust Novel Ene-Reductases from Thermophilic Fungi
by Pedro H. Damada and Marco W. Fraaije
Catalysts 2024, 14(11), 764; https://doi.org/10.3390/catal14110764 - 29 Oct 2024
Viewed by 512
Abstract
Ene-reductases (ERs) are enzymes known for catalyzing the asymmetric hydrogenation of activated alkenes. Among these, old yellow enzyme (OYE) ERs have been the most extensively studied for biocatalytic applications due to their dependence on NADH or NADPH as electron donors. These flavin-containing enzymes [...] Read more.
Ene-reductases (ERs) are enzymes known for catalyzing the asymmetric hydrogenation of activated alkenes. Among these, old yellow enzyme (OYE) ERs have been the most extensively studied for biocatalytic applications due to their dependence on NADH or NADPH as electron donors. These flavin-containing enzymes are highly enantio- and stereoselective, making them attractive biocatalysts for industrial use. To discover novel thermostable OYE-type ERs, we explored genomes of thermophilic fungi. Five genes encoding ERs were selected and expressed in Escherichia coli, namely AtOYE (from Aspergillus thermomutatus), CtOYE (from Chaetomium thermophilum), LtOYE (from Lachancea thermotolerans), OpOYE (from Ogatae polymorpha), and TtOYE (from Thermothielavioides terrestris). Each enzyme was purified as a soluble FMN-containing protein, allowing detailed characterization. All ERs exhibited a preference for NADPH, with AtOYE showing the broadest substrate range. Moreover, all the enzymes showed activity toward maleimide and p-benzoquinone, with TtOYE presenting the highest catalytic efficiency. The optimal pH for enzyme activity was between 6 and 7 and the enzymes displayed notable solvent tolerance and thermostability, with CtOYE and OpOYE showing the highest stability (Tm > 60 °C). Additionally, all enzymes converted R-carvone into (R,R)-dihydrocarvone. In summary, this study contributes to expanding the toolbox of robust ERs. Full article
(This article belongs to the Special Issue Enzyme and Biocatalysis Application)
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Graphical abstract

Graphical abstract
Full article ">Figure 1
<p>Asymmetric reduction of activated alkenes by ene–reductases (ERs).</p> Full article ">Figure 2
<p>Phylogenic tree constructed using the protein sequences selected for this study and ERs described in the literature [<a href="#B7-catalysts-14-00764" class="html-bibr">7</a>]. The analysis involved 79 protein sequences. The enzymes of this study (AtOYE, CtOYE, LtOYE, OpOYE, and TtOYE) are tagged by small orange dots. OYE1 is tagged with a small yellow dot.</p> Full article ">Figure 3
<p>Sequence alignment of AtOYE, CtOYE, LtOYE, OpOYE, TtOYE, and OYE1. Two regions are highlighted (yellow and gray shade), representing the patterns indicative for monomeric ERs, active site residues are in blue, and FMN-binding residues are in green letters. The letters in red were used to highlight amino acids different from OYE1. The symbol (*) denotes full conservation (identical residues across all sequences), (:) indicates strong conservation (similar residues with high chemical similarity), and (.) represents weak conservation (similar residues with low chemical similarity).</p> Full article ">Figure 4
<p>Structures for AtOYE (<b>A</b>), CtOYE (<b>B</b>), LtOYE (<b>C</b>), OpOYE (<b>D</b>), TtOYE (<b>E</b>), and OYE1 (<b>F</b>), as predicted by AlphaFold2 (v2.3.1, DeepMind, London, UK). The figures were generated using Pymol (v2.5.2, Schrödinger, Inc., New York, NY, USA).</p> Full article ">Figure 4 Cont.
<p>Structures for AtOYE (<b>A</b>), CtOYE (<b>B</b>), LtOYE (<b>C</b>), OpOYE (<b>D</b>), TtOYE (<b>E</b>), and OYE1 (<b>F</b>), as predicted by AlphaFold2 (v2.3.1, DeepMind, London, UK). The figures were generated using Pymol (v2.5.2, Schrödinger, Inc., New York, NY, USA).</p> Full article ">Figure 5
<p>Absorbance spectra obtained for AtOYE (<b>A</b>), CtOYE (<b>B</b>), LtOYE (<b>C</b>), OpOYE (<b>D</b>), and TtOYE (<b>E</b>). The continued line (–) represents the spectra of the native enzymes, and the spectra with the dashed line (--) were obtained upon unfolding.</p> Full article ">Figure 6
<p>pH optima for AtOYE (<b>A</b>), CtOYE (<b>B</b>), LtOYE (<b>C</b>), OpOYE (<b>D</b>), and TtOYE (<b>E</b>).</p> Full article ">Figure 7
<p>Effect of solvents on melting temperatures of ERs.</p> Full article ">Figure 8
<p>Melting temperatures (T<sub>m</sub>) measured for ERs at different pH values.</p> Full article ">
12 pages, 1191 KiB  
Article
Enzymatic Production of Chitooligosaccharide Using a GH Family 46 Chitosanase from Paenibacillus elgii and Its Antioxidant Activity
by Chien Thang Doan, Thi Ngoc Tran, Anh Dzung Nguyen and San-Lang Wang
Catalysts 2024, 14(11), 761; https://doi.org/10.3390/catal14110761 - 29 Oct 2024
Viewed by 390
Abstract
Chitooligosaccharide (COS), a natural antioxidant, is a hydrolysis product of chitosan created using enzymatic or chemical methods. COS has received considerable attention recently, making its efficient bioproduction of great value. This study investigated the optimal conditions for the enzymatic method using a GH [...] Read more.
Chitooligosaccharide (COS), a natural antioxidant, is a hydrolysis product of chitosan created using enzymatic or chemical methods. COS has received considerable attention recently, making its efficient bioproduction of great value. This study investigated the optimal conditions for the enzymatic method using a GH family 46 chitosanase from Paenibacillus elgii TKU051 to prepare COS based on the response surface methodology (RSM). The results showed optimal values for chitosan hydrolysis, such as a pH of 5.5, an incubation temperature of 58.3 °C, an [E]/[S] ratio of 118.494 (U/g), and an incubation time of 6.821 h. Under the optimal conditions, the highest reducing sugar level (per substrate, w/w) of the chitosan hydrolysis process that could be reached was 690.587 mg/g. The composition of the obtained COS was analyzed using the thin-layer chromatography (TLC) method, yielding (GlcN)2 and (GlcN)3 as the products. The ascorbic acid equivalent antioxidant capacity (AEAC) of the obtained COS was found to be 1246 mg/100 g (via a DPPH (2,2-diphenyl-1-picrylhydrazyl) radical-scavenging assay) and 3673 mg/100 g (via an ABTS (2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)) radical-scavenging assay). This green and efficient bioproduction method may possess excellent potential for application in bioactive COS preparation. Full article
(This article belongs to the Special Issue Enzyme and Biocatalysis Application)
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Graphical abstract

Graphical abstract
Full article ">Figure 1
<p>Effect of pH (<b>a</b>), temperature (<b>b</b>), [E]/[S] ratio (<b>c</b>), and incubation time (<b>d</b>) on reducing sugar produced from chitosan hydrolysis using <span class="html-italic">P. elgii</span> TKU051 chitosanase.</p> Full article ">Figure 2
<p>Normal probability plot of standardized residuals (<b>a</b>) and standardized residuals vs. predicted values (<b>b</b>).</p> Full article ">Figure 3
<p>Presented are 3D response surface plots for the effects of four primary factors on reducing sugar: (<b>a</b>) pH (A) vs. temperature (B, °C); (<b>b</b>) pH (A) vs. [E]/[S] ratio (C, U/g); (<b>c</b>) pH (A) vs. incubation time (D, h); (<b>d</b>) temperature (B, °C) vs. [E]/[S] ratio (C, U/g); (<b>e</b>) temperature (B, °C) vs. incubation time (D, h); and (<b>f</b>) [E]/[S] ratio (C, U/g) vs. incubation time (D, h).</p> Full article ">Figure 4
<p>The thin-layer chromatography profile of chitosan hydrolysate catalyzed by <span class="html-italic">Paenibacillus elgii</span> TKU051 chitosanase. 1, standard chitosan oligosacharides; 2, chitosan hydrolysate.</p> Full article ">Figure 5
<p>Antioxidant profiles of COSs: DPPH radical-scavenging activity (<b>a</b>), and ABTS radical-scavenging activity (<b>b</b>).</p> Full article ">
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