Recent Advances in Oxidoreductases Biochemistry and Biotechnology

Topic Information

Dear Colleagues,

We are now accepting submissions for the MDPI Topic “Recent Advances in Oxidoreductases Biochemistry and Biotechnology”. Original research articles, reviews, and commentaries are welcome.

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

This MDPI Topic 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. We look forward to receiving your submissions.

Prof. Dr. Grzegorz Janusz
Dr. Anna Pawlik
Dr. Clemens Karl Peterbauer
Topic Editors

Keywords

Participating Journals

Journal Name	Impact Factor	CiteScore	Launched Year	First Decision (median)	APC
Antioxidants antioxidants	6.0	10.6	2012	16.9 Days	CHF 2900
BioChem biochem	-	-	2021	21.7 Days	CHF 1000
Biomolecules biomolecules	4.8	9.4	2011	18.4 Days	CHF 2700
Cells cells	5.1	9.9	2012	17 Days	CHF 2700
Molecules molecules	4.2	7.4	1996	15.1 Days	CHF 2700
International Journal of Molecular Sciences ijms	4.9	8.1	2000	16.8 Days	CHF 2900
Methods and Protocols mps	2.3	3.6	2018	30.6 Days	CHF 1800

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Published Papers (3 papers)

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All Antioxidants BioChem Biomolecules Cells Molecules IJMS MPs

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Supplementary material:
Supplementary File 1 (ZIP, 286 KiB)

26 pages, 2294 KiB  

Open AccessEditor’s ChoiceProtocol

The Multifunctional Catalytic Hemoglobin from Amphitrite ornata: Protocols on Isolation, Taxonomic Identification, Protein Extraction, Purification, and Characterization

by Anna L. Husted, Victoria R. Sutton, Lauren A. Presnar, R. Kevin Blackburn, Joseph L. Staton, Stephen A. Borgianini and Edward L. D’Antonio

Methods Protoc. 2024, 7(6), 100; https://doi.org/10.3390/mps7060100 - 11 Dec 2024

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Abstract

The multifunctional catalytic hemoglobin from the terebellid polychaete Amphitrite ornata, also named dehaloperoxidase (AoDHP), utilizes the typical oxygen transport function in addition to four observed activities involved in substrate oxidation. The multifunctional ability of AoDHP is presently a rare [...] Read more.

The multifunctional catalytic hemoglobin from the terebellid polychaete Amphitrite ornata, also named dehaloperoxidase (AoDHP), utilizes the typical oxygen transport function in addition to four observed activities involved in substrate oxidation. The multifunctional ability of AoDHP is presently a rare observation, and there exists a limitation for how novel dehaloperoxidases can be identified from macrobenthic infauna. In order to discover more infaunal DHP-bearing candidates, we have devised a facilitated method for an accurate taxonomic identification that places visual and molecular taxonomic approaches in parallel. Traditional visual taxonomic species identification by the non-specialist, at least for A. ornata or even for other marine worms, is a very difficult and time-consuming task since a large diversity is present and the method is restricted to adult worm specimens. The work herein aimed to describe a method that simplifies the taxonomic identification of A. ornata in particular through the assessment of its mitochondrial cytochrome c oxidase subunit I gene by employing the DNA barcoding technique. Furthermore, whole-worm specimens of A. ornata were used to extract and purify AoDHP followed by an H₂O₂-dependent peroxidase activity assay evaluation against substrate 2,4,6-trichlorophenol. AoDHP isoenzyme A was also overexpressed as the recombinant protein in Escherichia coli, and its peroxidase activity parameters were compared to AoDHP from the natural source. The activity assay assessment indicated a tight correlation for all Michaelis–Menten parameters evaluated. We conclude that the method described herein exhibits a streamlined approach to identify the polychaete A. ornata, which can be adopted by the non-specialist, and the full procedure is predicted to facilitate the discovery of novel dehaloperoxidases from other marine invertebrates. Full article

(This article belongs to the Topic Recent Advances in Oxidoreductases Biochemistry and Biotechnology)

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15 pages, 2235 KiB  

Open AccessArticle

Characterization of a Pyranose Oxidase/C-Glycoside Oxidase from Microbacterium sp. 3H14, Belonging to the Unexplored Clade II of Actinobacterial POx/CGOx

by Andrea Martschini, Anja Kostelac, Dietmar Haltrich and Clemens K. Peterbauer

Biomolecules 2024, 14(12), 1510; https://doi.org/10.3390/biom14121510 - 26 Nov 2024

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Abstract

Pyranose oxidase (POx) is an FAD-dependent oxidoreductase and belongs to the glucose–methanol–choline (GMC) superfamily of oxidoreductases. As recently reported, POxs and FAD-dependent C-glycoside oxidases (CGOxs) share the same sequence space, and phylogenetic analysis of actinobacterial sequences belonging to this shared sequence space [...] Read more.

Pyranose oxidase (POx) is an FAD-dependent oxidoreductase and belongs to the glucose–methanol–choline (GMC) superfamily of oxidoreductases. As recently reported, POxs and FAD-dependent C-glycoside oxidases (CGOxs) share the same sequence space, and phylogenetic analysis of actinobacterial sequences belonging to this shared sequence space showed that it can be divided into four clades. Here, we report the biochemical characterization of a POx/CGOx from Microbacterium sp. 3H14 (MPOx), belonging to the hitherto unexplored clade II of actinobacterial POx/CGOx. Overall, MPOx demonstrates comparable features to POxs/CGOxs of clades III and IV, including the preference for glycosides over monosaccharides as electron donors. However, as MPOx efficiently oxidizes the C-glycoside aspalathin as well as the O-glycoside phlorizin, it shows activity with yet another set of glycoside structures compared to other POx/CGOx members. Full article

(This article belongs to the Topic Recent Advances in Oxidoreductases Biochemistry and Biotechnology)

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11 pages, 524 KiB  

Open AccessArticle

Novel Basidiomycetous Alcohol Oxidase from Cerrena unicolor—Characterisation, Kinetics, and Proteolytic Modifications

by Sylwia Stefanek, Rafał Typek, Michał Dybowski, Dorota Wianowska, Magdalena Jaszek and Grzegorz Janusz

Int. J. Mol. Sci. 2024, 25(22), 11890; https://doi.org/10.3390/ijms252211890 - 5 Nov 2024

Viewed by 676

Abstract

Intracellular alcohol oxidase (AOX) was isolated from the basidiomycetous white rot fungus Cerrena unicolor FCL139. The enzyme was semi-purified (13-fold) using two-step chromatography with 30% activity recovery. The identity of the protein was confirmed by LC-MS/MS analysis, and its MW (72 kDa) and [...] Read more.

Intracellular alcohol oxidase (AOX) was isolated from the basidiomycetous white rot fungus Cerrena unicolor FCL139. The enzyme was semi-purified (13-fold) using two-step chromatography with 30% activity recovery. The identity of the protein was confirmed by LC-MS/MS analysis, and its MW (72 kDa) and pI (6.18) were also determined. The kinetics parameters of the AOX reaction towards various substrates were analysed, which proved that, in addition to methanol (4.36 ± 0.27% of the oxidised substrate), AOX most potently oxidises aromatic alcohols, such as 4-hydroxybenzyl alcohol (14.0 ± 0.8%), benzyl alcohol (4.2 ± 0.3%), anisyl alcohol (7.6 ± 0.4%), and veratryl alcohol (5.0 ± 0.3%). Moreover, the influence of selected commercially available proteases on the biocatalytic properties of AOX from C. unicolor was studied. It was proved that the digested enzyme lost its catalytic potential properties except when incubated with pepsin, which significantly boosted its activity up to 123%. Full article

(This article belongs to the Topic Recent Advances in Oxidoreductases Biochemistry and Biotechnology)

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