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

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

Deadline for manuscript submissions: closed (20 September 2022) | Viewed by 12729

Special Issue Editors

Dr. Yan Zhang

E-Mail Website
Guest Editor
Department of Biological and Chemical Engineering, Faculty of Technical Sciences, Aarhus University, Gustav Wieds Vej 10, 8000 Aarhus, Denmark
Interests: biocatalysis; enzyme Engineering; bioactive Compounds; biodegradation
Dr. Raushan Kumar Singh

E-Mail Website
Guest Editor
Department of Biological and Chemical Engineering, Section of Industrial Biotechnology, Aarhus University, Aarhus, Denmark
Interests: enzyme discovery and engineering enzymes with focus on structure-function relationship; protein chemistry; enzyme catalyzed reactions for biosynthesis; multienzyme cascade reaction

Special Issue Information

Dear Colleagues,

Enzymes as natural catalysts have been widely used in various fields, including pharmaceuticals, food manufacturing, biofuels, cosmetic products, and as tools for research and development. Enzyme catalysis has been developed into a rather mature technology and as an alternative to chemical catalysis in recent decades, especially to make chiral compounds for pharmaceuticals as well for chemically challenging reactions. Supported by modern bioinformatics and computer-assisted enzyme discovery and engineering, abundant new enzymes or variants with excellent properties have been rapidly identified for numerous applications.

This Special Issue intends to discuss the advances, state-of-the-art techniques, limitations and opportunities and provide an outlook on the development and improvement of enzyme catalysis. We aim to collect a set of original research articles and reviews that cover all aspects of enzyme catalysis.

Dr. Yan Zhang
Dr. Raushan Kumar Singh
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

  • enzyme catalysis
  • industrial applications
  • enzyme discovery
  • enzyme engineering
  • techniques

Published Papers (6 papers)

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Research

12 pages, 1900 KiB  
Article
Production of Fructooligosaccharides Using a Commercial Heterologously Expressed Aspergillus sp. Fructosyltransferase
by Klaudia Karkeszová and Milan Polakovič
Catalysts 2023, 13(5), 843; https://0-doi-org.brum.beds.ac.uk/10.3390/catal13050843 - 06 May 2023
Cited by 1 | Viewed by 1770
Abstract
The catalytic properties of Seqenzym® FT, a fungal fructosyltransferase heterologously expressed in yeasts, were investigated at a temperature of 55 °C and pH 5.5. The initial rate measurements showed that the transfructosylation rate was only slightly inhibited by sucrose above the concentration [...] Read more.
The catalytic properties of Seqenzym® FT, a fungal fructosyltransferase heterologously expressed in yeasts, were investigated at a temperature of 55 °C and pH 5.5. The initial rate measurements showed that the transfructosylation rate was only slightly inhibited by sucrose above the concentration of 1.5 M. A rather low level of hydrolytic side activity was observed even at sucrose concentrations as low as 0.25 M. In progress curve experiments, the mass yield of fructooligosaccharides (FOS) reached a maximum value of 57% at this sucrose concentration, although it dropped to about 35% later on. At high initial sucrose concentrations up to 2 M, the FOS yield reached a maximum value of approximately 63% at a sucrose conversion of approximately 90%. Although neither the yield nor the conversion changed much later on, the progress of the reaction was manifested by the gradual depletion of shorter chain FOS, 1-kestose and nystose, and the accumulation of 1-β-fructofuranosyl nystose. At initial sucrose concentrations of 2 M, the degree of polymerization expressed through the number of fructosyl units grew from 2.3 at a conversion degree of 87% to 3.1 at a conversion degree of 94%. Compared to other commercial preparations, Seqenzym® FT can better produce FOS with a higher degree of polymerization. Full article
(This article belongs to the Special Issue Enzyme Catalysis: Advances, Techniques and Outlooks)
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11 pages, 1637 KiB  
Article
Enzymatic Synthesis of Ascorbic Acid-Ketone Body Hybrids
by Valentina Venturi, Lindomar Alberto Lerin, Francesco Presini, Pier Paolo Giovannini, Martina Catani, Alessandro Buratti, Nicola Marchetti, Latha Nagamani Dilliraj and Simona Aprile
Catalysts 2023, 13(4), 691; https://0-doi-org.brum.beds.ac.uk/10.3390/catal13040691 - 01 Apr 2023
Cited by 1 | Viewed by 1320
Abstract
Molecular hybrids obtained by connecting two or more bioactive molecules through a metabolizable linker are used as multi-target drugs for the therapy of multifactorial diseases. Ascorbic acid, as well as the ketone bodies acetoacetate and (R)-3-hydroxybutyrate, are bioactive molecules that have [...] Read more.
Molecular hybrids obtained by connecting two or more bioactive molecules through a metabolizable linker are used as multi-target drugs for the therapy of multifactorial diseases. Ascorbic acid, as well as the ketone bodies acetoacetate and (R)-3-hydroxybutyrate, are bioactive molecules that have common fields of application in the treatment and prevention of neurodegenerative diseases and cardiac injuries as well. In spite of this, the preparation of ascorbic acid ketone body hybrids is uncovered by the literature. Herein, we report the lipase-catalyzed condensation of methyl acetoacetate with ascorbic acid, which affords the 6-O-acetoacetyl ascorbic acid in quantitative yield. The same approach, employing the methyl (R)-3-hydroxybutyrate in place of the methyl acetoacetate, allows the preparation of the 6-O-(R)-3-hydroxybutyryl ascorbic acid in 57% yield. A better result (90% overall yield) is achieved through the lipase-catalyzed coupling of ascorbic acid with methyl (R)-3-O-methoxymethyl-3-hydroxybutyrate followed by the cleavage of the MOM protecting group. The two novel products are fully characterized and additional information on the antioxidant activity of the new products is also given. Full article
(This article belongs to the Special Issue Enzyme Catalysis: Advances, Techniques and Outlooks)
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8 pages, 1292 KiB  
Article
Novel Biotransformation of Maslinic Acid to MA-2-O-β-D-Glucoside by UDP-Glycosyltransferases from Bacillus subtilis
by Fen Hu, Jiaxin Chen, Yunfeng Zhang, Yuxi Sun, Yan Liu, Yuan Yu, Ke Xu and Haifeng Cai
Catalysts 2022, 12(8), 884; https://0-doi-org.brum.beds.ac.uk/10.3390/catal12080884 - 12 Aug 2022
Viewed by 1283
Abstract
Maslinic acid (MA) is a pentacyclic triterpenoid which originates from olive and other plants. Though MA possesses multiple biological activities, it has limitations due to its poor water solubility. YojK, YjiC, and UGT109A3 UDP-glycosyltransferases (UGTs) from Bacillus subtilis (B. subtilis) were [...] Read more.
Maslinic acid (MA) is a pentacyclic triterpenoid which originates from olive and other plants. Though MA possesses multiple biological activities, it has limitations due to its poor water solubility. YojK, YjiC, and UGT109A3 UDP-glycosyltransferases (UGTs) from Bacillus subtilis (B. subtilis) were utilized to catalyze the conjugation of MA with UDP-Glucose to generate a new MA glycosylation product, MA-2-O-β-D-glucoside (MA-2-O-β-D-Glu). The experimental results indicated that the resultant water solubility of MA-2-O-β-D-Glu is 1.69 times higher than that of MA. In addition, the recombinant YojK showed maximum activity at 40 °C with a pH range of 8.0−10.0, while the recombinant YjiC showed maximum activity at 45 °C with a pH of 8.0, and the recombinant UGT109A3 showed maximum activity at 40 °C with a pH of 8.0. Mg2+ is an important factor for efficient catalysis by three recombinant glycosyltransferases. The chemical conversion rate of the recombinant YojK, YjiC, and UGT109A3 is nearly 100% at their optimum pH, temperature, and metal ions. Furthermore, eight essential residues of three UGTs for MA glycosylation modification were further determined by molecular docking and site-directed mutagenesis. Thus, efficient glycosylation modification improves the water solubility of MA and provides a new potential method for the glycosylation modification of other pentacyclic triterpenoids. Full article
(This article belongs to the Special Issue Enzyme Catalysis: Advances, Techniques and Outlooks)
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12 pages, 4978 KiB  
Article
Engineered Stable 5-Hydroxymethylfurfural Oxidase (HMFO) from 8BxHMFO Variant of Methylovorus sp. MP688 through B-Factor Analysis
by Qiuyang Wu, Dong Lu, Shuming Jin, Jie Lu, Fang Wang, Luo Liu and Kaili Nie
Catalysts 2021, 11(12), 1503; https://0-doi-org.brum.beds.ac.uk/10.3390/catal11121503 - 10 Dec 2021
Cited by 7 | Viewed by 2622
Abstract
What is known as Furan-2,5-dicarboxylic acid (FDCA) is an attractive compound since it has similar properties to terephthalic acid. Further, 5-hydroxymethylfurfural oxidase (HMFO) is an enzyme, which could convert HMF to FDCA directly. Most wild types of HMFO have low activity on the [...] Read more.
What is known as Furan-2,5-dicarboxylic acid (FDCA) is an attractive compound since it has similar properties to terephthalic acid. Further, 5-hydroxymethylfurfural oxidase (HMFO) is an enzyme, which could convert HMF to FDCA directly. Most wild types of HMFO have low activity on the oxidation of HMF to FDCA. The variant of 8BxHFMO from Methylovorus sp. MP688 was the only reported enzyme that was able to perform FDCA production. However, the stabilization of 8BxHMFO is still not that satisfactory, and further improvement is necessary for the industrial application of the enzyme. In this work, stability-enhanced HMFO from 8BxHFMO was engineered through employing B-factor analysis. The mutation libraries were created based on the NNK degeneracy of residues with the top ten highest B-factor value, and two of the effective mutants were screened out through the high throughput selection with the horseradish peroxidase (HRP)-Tyr assay. The mutants Q319K and N44G show a significantly increased yield of FDCA in the reaction temperature range of 30 to 40 °C. The mutant Q319K shows the best performance at 35 °C with a FDCA yield of 98% (the original 8BxHMFO was only 85%), and a half-life exceeding 72 h. Moreover, molecular dynamic simulation indicates that more hydrogen bonds are formed in the mutants, which improves the stability of the protein structure. The method could enhance the design of more stable biocatalysts; and provides potential for the further optimization and utilization of HMFO in biotechnological processes. Full article
(This article belongs to the Special Issue Enzyme Catalysis: Advances, Techniques and Outlooks)
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10 pages, 1282 KiB  
Article
Chemoenzymatic Stereodivergent Synthesis of All the Possible Stereoisomers of the 2,3-Dimethylglyceric Acid Ethyl Ester
by Francesco Presini, Graziano Di Carmine, Pier Paolo Giovannini, Virginia Cristofori, Lindomar Alberto Lerin, Olga Bortolini, Claudio Trapella and Anna Fantinati
Catalysts 2021, 11(12), 1440; https://0-doi-org.brum.beds.ac.uk/10.3390/catal11121440 - 26 Nov 2021
Cited by 2 | Viewed by 1632
Abstract
2,3-dihydroxy-2-methylbutyric acid, also known as 2,3-dimethylglyceric acid, constitutes the acyl and/or the alcoholic moiety of many bioactive natural esters. Herein, we describe a chemoenzymatic methodology which gives access to all the four possible stereoisomers of the 2,3-dimethylglyceric acid ethyl ester. The racemic ethyl [...] Read more.
2,3-dihydroxy-2-methylbutyric acid, also known as 2,3-dimethylglyceric acid, constitutes the acyl and/or the alcoholic moiety of many bioactive natural esters. Herein, we describe a chemoenzymatic methodology which gives access to all the four possible stereoisomers of the 2,3-dimethylglyceric acid ethyl ester. The racemic ethyl α-acetolactate, produced by the N-heterocycle carbene (NHC)-catalyzed coupling of ethyl pyruvate and methylacetoin was employed as the starting material. The racemic mixture was resolved through (S)-selective reductions, promoted by the acetylacetoin reductase (AAR) affording the resulting ethyl (2R,3S)-2,3-dimethylglycerate; the isolated remaining (S)-ethyl α-acetolactate was successively treated with baker’s yeast to obtain the corresponding (2S,3S) stereoisomer. syn-2,3-Dimethylgliceric acid ethyl ester afforded by reducing the rac-α-acetolactate with NaBH4 in the presence of ZnCl2 was kinetically resolved through selective acetylation with lipase B from Candida antarctica (CAL-B) and vinyl acetate to access to (2S,3R) stereoisomer. Finally, the (2R,3R) stereoisomer, was prepared by C3 epimerization of the (2R,3S) stereoisomer recovered from the above kinetic resolution, achieved through the TEMPO-mediated oxidation, followed by the reduction of the produced ketone with NaBH4. The resulting 2,3-dimethylglycertate enriched in the (2R,3R) stereoisomer was submitted to stereospecicific acetylation with vinyl acetate and CAL-B in order to separate the major stereoisomer. The entire procedure enabled conversion of the racemic α-acetolactate into the four enantiopure stereoisomers of the ethyl 2,3-dihydroxy-2-methylbutyrate with the following overall yields: 42% for the (2R,3S), 40% for the (2S,3S), 42% for the (2S,3R) and 20% for the (2R,3R). Full article
(This article belongs to the Special Issue Enzyme Catalysis: Advances, Techniques and Outlooks)
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14 pages, 2756 KiB  
Article
Synthesis of Linoleic Acid 13-Hydroperoxides from Safflower Oil Utilizing Lipoxygenase in a Coupled Enzyme System with In-Situ Oxygen Generation
by Valentin Gala Marti, Anna Coenen and Ulrich Schörken
Catalysts 2021, 11(9), 1119; https://0-doi-org.brum.beds.ac.uk/10.3390/catal11091119 - 17 Sep 2021
Cited by 7 | Viewed by 3115
Abstract
Linoleic acid hydroperoxides are versatile intermediates for the production of green note aroma compounds and bifunctional ω-oxo-acids. An enzyme cascade consisting of lipoxygenase, lipase and catalase was developed for one-pot synthesis of 13-hydroperoxyoctadecadienoic acid starting from safflower oil. Reaction conditions were optimized for [...] Read more.
Linoleic acid hydroperoxides are versatile intermediates for the production of green note aroma compounds and bifunctional ω-oxo-acids. An enzyme cascade consisting of lipoxygenase, lipase and catalase was developed for one-pot synthesis of 13-hydroperoxyoctadecadienoic acid starting from safflower oil. Reaction conditions were optimized for hydroperoxidation using lipoxygenase 1 from Glycine max (LOX-1) in a solvent-free system. The addition of green surfactant Triton CG-110 improved the reaction more than two-fold and yields of >50% were obtained at linoleic acid concentrations up to 100 mM. To combine hydroperoxidation and oil hydrolysis, 12 lipases were screened for safflower oil hydrolysis under the reaction conditions optimized for LOX-1. Lipases from Candida rugosa and Pseudomonas fluorescens were able to hydrolyze safflower oil to >75% within 5 h at a pH of 8.0. In contrast to C. rugosa lipase, the enzyme from P. fluorescens did not exhibit a lag phase. Combination of P. fluorescens lipase and LOX-1 worked well upon LOX-1 dosage and a synergistic effect was observed leading to >80% of hydroperoxides. Catalase from Micrococcus lysodeikticus was used for in-situ oxygen production with continuous H2O2 dosage in the LOX-1/lipase reaction system. Foam generation was significantly reduced in the 3-enzyme cascade in comparison to the aerated reaction system. Safflower oil concentration was increased up to 300 mM linoleic acid equivalent and 13-hydroperoxides could be produced in a yield of 70 g/L and a regioselectivity of 90% within 7 h. Full article
(This article belongs to the Special Issue Enzyme Catalysis: Advances, Techniques and Outlooks)
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