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Characterization of a novel AA16 lytic polysaccharide monooxygenase from Thermothelomyces thermophilus and comparison of biochemical properties with an LPMO from AA9 family.
Chorozian, Koar; Karnaouri, Anthi; Tryfona, Theodora; Kondyli, Nefeli Georgaki; Karantonis, Antonis; Topakas, Evangelos.
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  • Chorozian K; Ιndustrial Biotechnology & Biocatalysis Group, School of Chemical Engineering, National Technical University of Athens, Zografou Campus, 15772, Greece.
  • Karnaouri A; Laboratory of General and Agricultural Microbiology, Department of Crop Science, Agricultural University of Athens, Athens 11855, Greece. Electronic address: akarnaouri@aua.gr.
  • Tryfona T; Department of Biochemistry, School of Biological Sciences, University of Cambridge, Cambridge CB2 1QW, UK.
  • Kondyli NG; Ιndustrial Biotechnology & Biocatalysis Group, School of Chemical Engineering, National Technical University of Athens, Zografou Campus, 15772, Greece; Laboratory of Physical Chemistry and Applied Electrochemistry, School of Chemical Engineering, National Technical University of Athens, Zog
  • Karantonis A; Laboratory of Physical Chemistry and Applied Electrochemistry, School of Chemical Engineering, National Technical University of Athens, Zografou Campus, 15780, Greece.
  • Topakas E; Ιndustrial Biotechnology & Biocatalysis Group, School of Chemical Engineering, National Technical University of Athens, Zografou Campus, 15772, Greece. Electronic address: vtopakas@chemeng.ntua.gr.
Carbohydr Polym ; 342: 122387, 2024 Oct 15.
Article en En | MEDLINE | ID: mdl-39048228
ABSTRACT
Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes which are categorized in the CAZy database under auxiliary activities families AA9-11, 13, 14-17. Secreted by various microorganisms, they play a crucial role in carbon recycling, particularly in fungal saprotrophs. LPMOs oxidize polysaccharides through monooxygenase/peroxygenase activities and exhibit peroxidase and oxidase activities, with variations among different families. AA16, a newly identified LPMO family, is noteworthy due to limited studies on its members, thus rendering the characterization of AA16 enzymes vital for addressing controversies around their functions. This study focused on heterologous expression and biochemical study of an AA16 LPMO from Thermothelomyces thermophilus (formerly known as Myceliophthora thermophila), namely MtLPMO16A. Substrate specificity evaluation of MtLPMO16A showed oxidative cleavage of hemicellulosic substrates and no activity on cellulose, accompanied by a strong oxidase activity. A comparative analysis with an LPMO from AA9 family explored correlations between these families, while MtLPMO16A was shown to boost the activity of some AA9 family LPMOs. The results offer new insights into the AA16 family's action mode and microbial hemicellulose decomposition mechanisms in nature.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Polisacáridos / Oxigenasas de Función Mixta Idioma: En Revista: Carbohydr Polym Año: 2024 Tipo del documento: Article País de afiliación: Grecia Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Polisacáridos / Oxigenasas de Función Mixta Idioma: En Revista: Carbohydr Polym Año: 2024 Tipo del documento: Article País de afiliación: Grecia Pais de publicación: Reino Unido