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Biotechnological Applications of Oxidoreductases

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A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (30 April 2023) | Viewed by 15320

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Dr. Rebecca Pogni

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Guest Editor

Department of Biotechnology, Chemistry and Pharmacy, University of Siena, 53100 Siena, Italy
Interests: oxidative enzymes; metalloproteins; biocatalysis; protein radicals; lignin; fiber; electron paramagnetic resonance (EPR); enzyme immobilization; chitinolytic materials; biomaterials
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Dr. Maria Camilla Baratto

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Department of Biotechnology, Chemistry and Pharmacy, Università degli Studi di Siena, 53100 Siena, Italy
Interests: Eumelanin; Pyrrole-2,3,5-Tricarboxylic Acid; Auricularia Auricula-Judae

Special Issue Information

Dear Colleagues,

The submission of manuscripts is now welcome for the Special Issue “Biotechnological applications of oxidoreductases”, which will contain a selection of papers dealing with biotechnological applications of oxidoreductases. Original research reports, review articles, and commentaries are welcome.

Oxidoreductases comprise a large number of enzymes of industrial relevance: peroxidases, peroxygenases, laccases, flavin-containing oxidases ad dehydrogenases, unspecific peroxygenases (UPOs), dye-decolorizing peroxidases (DyPs), copper-containing lytic polysaccharide monooxygenases (LPMOs), etc.

This Special Issue aims to cover all aspects, from the discovery of novel oxidoreductases, mechanisms of action, and structure–activity relationships to their applications in the production of fine chemicals and polymer building blocks, biosensors, biomaterials, and use in biorefineries for a bio-based economy.

Dr. Rebecca Pogni
Dr. Maria Camilla Baratto
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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

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Keywords

oxidoreductases
peroxidases
peroxygenases
laccases
flavin-containing oxidases ad dehydrogenases
unspecific peroxygenases (UPOs)
dye-decolorizing peroxidases (DyPs)
copper-containing lytic polysaccharide monooxygenases (LPMOs)
lignocellulose residues

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Published Papers (7 papers)

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Editorial

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2 pages, 161 KiB

Open AccessEditorial

Special Issue on Biotechnological Applications of Oxidoreductases

by Maria Camilla Baratto and Rebecca Pogni

Int. J. Mol. Sci. 2024, 25(3), 1758; https://doi.org/10.3390/ijms25031758 - 1 Feb 2024

Viewed by 715

Abstract

This Special Issue was launched in conjunction with the 10th edition of the OxiZymes meeting in Siena (Italy) in 2022 [...] Full article

(This article belongs to the Special Issue Biotechnological Applications of Oxidoreductases)

Research

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18 pages, 3704 KiB

Open AccessArticle

Spectrophotometric Assay for the Detection of 2,5-Diformylfuran and Its Validation through Laccase-Mediated Oxidation of 5-Hydroxymethylfurfural

by Nicoletta Cascelli, Vicente Gotor-Fernández, Iván Lavandera, Giovanni Sannia and Vincenzo Lettera

Int. J. Mol. Sci. 2023, 24(23), 16861; https://doi.org/10.3390/ijms242316861 - 28 Nov 2023

Viewed by 1703

Abstract

Modern biocatalysis requires fast, sensitive, and efficient high-throughput screening methods to screen enzyme libraries in order to seek out novel biocatalysts or enhanced variants for the production of chemicals. For instance, the synthesis of bio-based furan compounds like 2,5-diformylfuran (DFF) from 5-hydroxymethylfurfural (HMF) via aerobic oxidation is a crucial process in industrial chemistry. Laccases, known for their mild operating conditions, independence from cofactors, and versatility with various substrates, thanks to the use of chemical mediators, are appealing candidates for catalyzing HMF oxidation. Herein, Schiff-based polymers based on the coupling of DFF and 1,4-phenylenediamine (PPD) have been used in the set-up of a novel colorimetric assay for detecting the presence of DFF in different reaction mixtures. This method may be employed for the fast screening of enzymes (Z’ values ranging from 0.68 to 0.72). The sensitivity of the method has been proved, and detection (8.4 μM) and quantification (25.5 μM) limits have been calculated. Notably, the assay displayed selectivity for DFF and enabled the measurement of kinetics in DFF production from HMF using three distinct laccase–mediator systems. Full article

(This article belongs to the Special Issue Biotechnological Applications of Oxidoreductases)

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16 pages, 5767 KiB

Open AccessArticle

Rational Design of Daunorubicin C-14 Hydroxylase Based on the Understanding of Its Substrate-Binding Mechanism

by Jing Zhang, Ling-Xiao Gao, Wei Chen, Jian-Jiang Zhong, Chao Qian and Wen-Wen Zhou

Int. J. Mol. Sci. 2023, 24(9), 8337; https://doi.org/10.3390/ijms24098337 - 6 May 2023

Cited by 2 | Viewed by 2345

Abstract

Doxorubicin is one of the most widely used antitumor drugs and is currently produced via the chemical conversion method, which suffers from high production costs, complex product separation processes, and serious environmental pollution. Biocatalysis is considered a more efficient and environment-friendly method for drug production. The cytochrome daunorubicin C-14 hydroxylase (DoxA) is the essential enzyme catalyzing the conversion of daunorubicin to doxorubicin. Herein, the DoxA from Streptomyces peucetius subsp. caesius ATCC 27952 was expressed in Escherichia coli, and the rational design strategy was further applied to improve the enzyme activity. Eight amino acid residues were identified as the key sites via molecular docking. Using a constructed screening library, we obtained the mutant DoxA(P88Y) with a more rational protein conformation, and a 56% increase in bioconversion efficiency was achieved by the mutant compared to the wild-type DoxA. Molecular dynamics simulation was applied to understand the relationship between the enzyme’s structural property and its substrate-binding efficiency. It was demonstrated that the mutant DoxA(P88Y) formed a new hydrophobic interaction with the substrate daunorubicin, which might have enhanced the binding stability and thus improved the catalytic activity. Our work lays a foundation for further exploration of DoxA and facilitates the industrial process of bio-production of doxorubicin. Full article

(This article belongs to the Special Issue Biotechnological Applications of Oxidoreductases)

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12 pages, 3363 KiB

Open AccessArticle

Studies on the Oxidation of Aromatic Amines Catalyzed by Trametes versicolor Laccase

by Ivan Bassanini, Simone Grosso, Chiara Tognoli, Giovanni Fronza and Sergio Riva

Int. J. Mol. Sci. 2023, 24(4), 3524; https://doi.org/10.3390/ijms24043524 - 9 Feb 2023

Cited by 4 | Viewed by 2228

Abstract

The bio-oxidation of a series of aromatic amines catalyzed by T. versicolor laccase has been investigated exploiting either commercially available nitrogenous substrates [(E)-4-vinyl aniline and diphenyl amine] or ad hoc synthetized ones [(E)-4-styrylaniline, (E)-4-(prop-1-en-1-yl)aniline and (E)-4-(((4-methoxyphenyl)imino)methyl)phenol]. At variance to their phenolic equivalents, the investigated aromatic amines were not converted into the expected cyclic dimeric structures under T. versicolor catalysis. The formation of complex oligomeric/polymeric or decomposition by-products was mainly observed, with the exception of the isolation of two interesting but unexpected chemical skeletons. Specifically, the biooxidation of diphenylamine resulted in an oxygenated quinone-like product, while, to our surprise, in the presence of T. versicolor laccase (E)-4-vinyl aniline was converted into a 1,2-substited cyclobutane ring. To the best of our knowledge, this is the first example of an enzymatically triggered [2 + 2] olefin cycloaddition. Possible reaction mechanisms to explain the formation of these products are also reported. Full article

(This article belongs to the Special Issue Biotechnological Applications of Oxidoreductases)

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15 pages, 2123 KiB

Open AccessArticle

Localization of Pyranose 2-Oxidase from Kitasatospora aureofaciens: A Step Closer to Elucidate a Biological Role

by Ludovika Jessica Virginia and Clemens Peterbauer

Int. J. Mol. Sci. 2023, 24(3), 1975; https://doi.org/10.3390/ijms24031975 - 19 Jan 2023

Cited by 5 | Viewed by 1813

Abstract

Lignin degradation in fungal systems is well characterized. Recently, a potential for lignin depolymerization and modification employing similar enzymatic activities by bacteria is increasingly recognized. The presence of genes annotated as peroxidases in Actinobacteria genomes suggests that these bacteria should contain auxiliary enzymes such as flavin-dependent carbohydrate oxidoreductases. The only auxiliary activity subfamily with significantly similar representatives in bacteria is pyranose oxidase (POx). A biological role of providing H₂O₂ for peroxidase activation and reduction of radical degradation products suggests an extracellular localization, which has not been established. Analysis of the genomic locus of POX from Kitasatospora aureofaciens (KaPOx), which is similar to fungal POx, revealed a start codon upstream of the originally annotated one, and the additional sequence was considered a putative Tat-signal peptide by computational analysis. We expressed KaPOx including this additional upstream sequence as well as fusion constructs consisting of the additional sequence, the KaPOx mature domain and the fluorescent protein mRFP1 in Streptomyces lividans. The putative signal peptide facilitated secretion of KaPOx and the fusion protein, suggesting a natural extracellular localization and supporting a potential role in providing H₂O₂ and reducing radical compounds derived from lignin degradation. Full article

(This article belongs to the Special Issue Biotechnological Applications of Oxidoreductases)

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15 pages, 2065 KiB

Open AccessArticle

Biochemical Characterization of Pyranose Oxidase from Streptomyces canus—Towards a Better Understanding of Pyranose Oxidase Homologues in Bacteria

by Anja Kostelac, Leander Sützl, Jolanta Puc, Valentina Furlanetto, Christina Divne and Dietmar Haltrich

Int. J. Mol. Sci. 2022, 23(21), 13595; https://doi.org/10.3390/ijms232113595 - 6 Nov 2022

Cited by 7 | Viewed by 2320

Abstract

Pyranose oxidase (POx, glucose 2-oxidase; EC 1.1.3.10, pyranose:oxygen 2-oxidoreductase) is an FAD-dependent oxidoreductase and a member of the auxiliary activity (AA) enzymes (subfamily AA3_4) in the CAZy database. Despite the general interest in fungal POxs, only a few bacterial POxs have been studied so far. Here, we report the biochemical characterization of a POx from Streptomyces canus (ScPOx), the sequence of which is positioned in a separate, hitherto unexplored clade of the POx phylogenetic tree. Kinetic analyses revealed that ScPOx uses monosaccharide sugars (such as d-glucose, d-xylose, d-galactose) as its electron-donor substrates, albeit with low catalytic efficiencies. Interestingly, various C- and O-glycosides (such as puerarin) were oxidized by ScPOx as well. Some of these glycosides are characteristic substrates for the recently described FAD-dependent C-glycoside 3-oxidase from Microbacterium trichothecenolyticum. Here, we show that FAD-dependent C-glycoside 3-oxidases and pyranose oxidases are enzymes belonging to the same sequence space. Full article

(This article belongs to the Special Issue Biotechnological Applications of Oxidoreductases)

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9 pages, 1266 KiB

Open AccessArticle

Improving Properties of Starch-Based Adhesives with Carboxylic Acids and Enzymatically Polymerized Lignosulfonates

by Miguel Jimenez Bartolome, Sidhant Satya Prakash Padhi, Oliver Gabriel Fichtberger, Nikolaus Schwaiger, Bernhard Seidl, Martin Kozich, Gibson S. Nyanhongo and Georg M. Guebitz

Int. J. Mol. Sci. 2022, 23(21), 13547; https://doi.org/10.3390/ijms232113547 - 4 Nov 2022

Cited by 8 | Viewed by 2831

Abstract

A novel strategy for improving wet resistance and bonding properties of starch-based adhesives using enzymatically polymerized lignosulfonates and carboxylic acids as additives was developed. Therefore, lignosulfonates were polymerized by laccase to a molecular weight of 750 kDa. Incorporation of low concentrations (up to 1% of the starch weight) of 1,2,3,4-butanetetracarboxylic acid (BTCA) led to further improvement on the properties of the adhesives, while addition of greater amounts of BTCA led to a decrease in the properties measured due to large viscosity increases. Great improvements in wet-resistance from 22 to 60 min and bonding times (from 30 to 20 s) were observed for an adhesive containing 8% enzymatically polymerized lignin and 1% BTCA. On the other hand, the addition of citric acid (CA) deteriorated the properties of the adhesives, especially when lignosulfonate was present. In conclusion, this study shows that the addition of the appropriate amount of enzymatically polymerized lignosulfonates together with carboxylic acids (namely BTCA) to starch-based adhesives is a robust strategy for improving their wet resistance and bonding times. Full article

(This article belongs to the Special Issue Biotechnological Applications of Oxidoreductases)

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