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	15.5 Days	CHF 2900
BioChem biochem	-	-	2021	24.1 Days	CHF 1000
Biomolecules biomolecules	4.8	9.4	2011	16.3 Days	CHF 2700
Cells cells	5.1	9.9	2012	17.5 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	18.1 Days	CHF 2900
Methods and Protocols mps	2.3	3.6	2018	24.9 Days	CHF 1800

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Published Papers (1 paper)

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All Antioxidants BioChem Biomolecules Cells Molecules IJMS MPs

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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

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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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