Topic Editors

Department of Biochemistry and Biotechnology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Akademicka 19 Street, 20-033 Lublin, Poland
Department of Biochemistry and Biotechnology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Lublin, Poland
Department of Food Sciences and Technology, BOKU—University of Natural Resources and Life Sciences, Vienna 1190, Austria

Recent Advances in Oxidoreductases Biochemistry and Biotechnology

Abstract submission deadline
closed (31 August 2024)
Manuscript submission deadline
closed (31 October 2024)
Viewed by
1618

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

  • oxidoreductases
  • microorganisms
  • enzymes
  • biocatalysis
  • oxizymes

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

Preprints.org is a multidiscipline platform providing preprint service that is dedicated to sharing your research from the start and empowering your research journey.

MDPI Topics is cooperating with Preprints.org and has built a direct connection between MDPI journals and Preprints.org. Authors are encouraged to enjoy the benefits by posting a preprint at Preprints.org prior to publication:

  1. Immediately share your ideas ahead of publication and establish your research priority;
  2. Protect your idea from being stolen with this time-stamped preprint article;
  3. Enhance the exposure and impact of your research;
  4. Receive feedback from your peers in advance;
  5. Have it indexed in Web of Science (Preprint Citation Index), Google Scholar, Crossref, SHARE, PrePubMed, Scilit and Europe PMC.

Published Papers (1 paper)

Order results
Result details
Journals
Select all
Export citation of selected articles as:
11 pages, 524 KiB  
Article
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 312
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
Show Figures

Figure 1

Back to TopTop