Characterization of a novel AA16 lytic polysaccharide monooxygenase from Thermothelomyces thermophilus and comparison of biochemical properties with an LPMO from AA9 family

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 oxidi...

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Bibliographic Details
Published in:Carbohydrate polymers 2024-10, Vol.342, p.122387, Article 122387
Main Authors: Chorozian, Koar, Karnaouri, Anthi, Tryfona, Theodora, Kondyli, Nefeli Georgaki, Karantonis, Antonis, Topakas, Evangelos
Format: Article
Language:English
Subjects:
AA16
Beechwood xylan
Electron donors
Fungal Proteins - chemistry
Fungal Proteins - genetics
Fungal Proteins - metabolism
LPMO
Mixed Function Oxygenases - chemistry
Mixed Function Oxygenases - genetics
Mixed Function Oxygenases - metabolism
Oxidase
Oxidoreductases
Polysaccharides - chemistry
Polysaccharides - metabolism
Sordariales - enzymology
Substrate Specificity
Thermothelomyces thermophilus
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Summary: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. [Display omitted]
ISSN:0144-8617
1879-1344
1879-1344
DOI:10.1016/j.carbpol.2024.122387