Special Issue on Biotechnological Applications of Oxidoreductases
Department of Biotechnology, Chemistry and Pharmacy, University of Siena, 53100 Siena, Italy
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Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2024, 25(3), 1758; https://doi.org/10.3390/ijms25031758
Submission received: 10 January 2024
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Revised: 23 January 2024
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Accepted: 29 January 2024
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Published: 1 February 2024
(This article belongs to the Special Issue Biotechnological Applications of Oxidoreductases)
This Special Issue was launched in conjunction with the 10th edition of the OxiZymes meeting in Siena (Italy) in 2022. Initially dedicated specifically to research on laccases and peroxidases, this series of conferences now cover the entire class of oxidoreductases. Oxidoreductases, which are enzymes catalyzing redox reactions, comprise a large number of enzymes of industrial relevance, including peroxidases, peroxygenases, laccases, flavin-containing oxidases, dehydrogenases, unspecific peroxygenases (UPOs), dye-decolorizing peroxidases (DyPs), and copper-containing lytic polysaccharide monooxygenases (LPMOs). Research on oxidoreductases covers different aspects ranging from discovering novel enzymes and conducting structure–activity relationship studies to exploring their applications in the production of fine chemicals and polymer building blocks, biosensors, and biomaterials for establishing a bio-based economy [1]. In chemical synthesis, oxidoreductases play an important role; the reaction routes are shorter, and for many of them, the chemical counterpart does not exist [2]. Furthermore, the generally mild reaction conditions may also reduce the environmental impact of the biocatalytic reactions compared to classical counterparts.
To cite some examples, laccases are copper-containing metalloenzymes that can be employed for the synthesis of fine chemicals, textile dyes, and development of novel green organic transformations [3,4,5]. Laccases engineered by directed evolution can also be applied for Kraft pulp biorefineries and fiberboard manufacture [6,7] whereas the mono-copper enzymes, currently named Lytic Polysaccharide MonoOxygenases (LPMOs), have intriguing and unprecedented catalytic properties. They can act as monooxygenases and peroxygenases in the oxidative cleavage of recalcitrant polysaccharides like cellulose and chitin [8]. Simultaneously, engineered flavoprotein oxidases exhibit interesting properties suitable for their use in industrial applications, as well as Unspecific Peroxygenases (UPO) and dye peroxidases (DyPs) [9,10,11].
In this Special Issue, papers related to the different biotechnological applications of oxidoreductases are reported.
Funding
This research received no external funding.
Conflicts of Interest
The authors declare no conflicts of interest.
References
- Martinez, A.T.; Ruiz-Dueñas, F.J.; Camarero, S.; Serrano, A.; Linde, D.; Lund, H.; Vind, J.; Tovborg, M.; Herold-Majumdar, O.M.; Hofrichter, M.; et al. Oxidoreductases on their way to industrial biotransformations. Biotechnol. Adv. 2017, 35, 815. [Google Scholar] [CrossRef] [PubMed]
- Dong, J.J.; Fernández-Fueyo, E.; Hollmann, F.; Paul, C.E.; Pesic, M.; Schmidt, S.; Wang, Y.; Younes, S.; Zhang, W. Biocatalytic Oxidation Reactions: A Chemist’s Perspective. Angew. Chem.-Int. Ed. 2018, 57, 9238. [Google Scholar] [CrossRef] [PubMed]
- Riva, S. Laccases: Blue Enzymes for Green Chemistry. Trends Biotechnol. 2006, 24, 219. [Google Scholar] [CrossRef] [PubMed]
- Polak, J.; Wlizło, K.; Pogni, R.; Petricci, E.; Grąz, M.; Szałapata, K.; Osińska-Jaroszuk, M.; Kapral-Piotrowska, J.; Pawlikowska-Pawlęga, B.; Jarosz-Wilkołazka, A. Structure and Bioactive Properties of Novel Textile Dyes Synthesised by Fungal Laccase. Int. J. Mol. Sci. 2020, 21, 2052. [Google Scholar] [CrossRef] [PubMed]
- Sousa, A.C.; Oliveira, M.C.; Martins, L.O.; Robalo, M.P. A Sustainable Synthesis of Asymmetric Phenazines and Phenoxazinones Mediated by CotA-LaccaseAdv. Synth. Catal. 2018, 360, 575. [Google Scholar] [CrossRef]
- Aza, P.; Camarero, S. Fungal Laccases: Fundamentals, Engineering and Classification Update. Biomolecules 2023, 13, 1716. [Google Scholar] [CrossRef] [PubMed]
- Rodríguez-Escribano, D.; de Salas, F.; Pliego, R.; Marques, G.; Levée, T.; Suonpää, A.; Gutiérres, A.; Martínez, Á.T.; Ihalainen, P.; Rencoret, J.; et al. Depolymerisation of Kraft Lignin by Tailor-Made Alkaliphilic Fungal Laccases. Polymers 2023, 15, 4433. [Google Scholar] [CrossRef] [PubMed]
- Sulaeva, I.; Budischowsky, D.; Rahikainen, J.; Marjamaa, K.; Støpamo, F.G.; Khaliliyan, H.; Melikhov, I.; Rosenau, T.; Kruus, K.; Várnai, A.; et al. A novel approach to analyze the impact of lytic polysaccharide monooxygenases (LPMOs) on cellulosic fibres. Carbohydr. Polym. 2024, 328, 121696. [Google Scholar] [CrossRef] [PubMed]
- Martin, C.; Binda, C.; Fraaije, M.W.; Mattevi, A. The multipurpose family of flavoprotein oxidases. Enzymes 2020, 47, 63. [Google Scholar] [CrossRef] [PubMed]
- Monterrey, D.T.; Menés-Rubio, A.; Keser, M.; Gonzalez-Perez, D.; Alcalde, M. Unspecific peroxygenases: The pot of gold at the end of the oxyfunctionalization rainbow? Curr. Opin. Green Sustain. Chem. 2023, 41, 100786. [Google Scholar] [CrossRef]
- Silva, D.; Rodrigues, C.F.; Lorena, C.; Borges, P.T.; Martins, L.O. Biocatalysis for biorefineries: The case of dye-decolorizing peroxidases. Biotechnol. Adv. 2023, 65, 108153. [Google Scholar] [CrossRef] [PubMed]
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Baratto, M.C.; Pogni, R. Special Issue on Biotechnological Applications of Oxidoreductases. Int. J. Mol. Sci. 2024, 25, 1758. https://doi.org/10.3390/ijms25031758
AMA Style
Baratto MC, Pogni R. Special Issue on Biotechnological Applications of Oxidoreductases. International Journal of Molecular Sciences. 2024; 25(3):1758. https://doi.org/10.3390/ijms25031758
Chicago/Turabian StyleBaratto, Maria Camilla, and Rebecca Pogni. 2024. "Special Issue on Biotechnological Applications of Oxidoreductases" International Journal of Molecular Sciences 25, no. 3: 1758. https://doi.org/10.3390/ijms25031758
APA StyleBaratto, M. C., & Pogni, R. (2024). Special Issue on Biotechnological Applications of Oxidoreductases. International Journal of Molecular Sciences, 25(3), 1758. https://doi.org/10.3390/ijms25031758
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