Light-stimulated T. thermophilus two-domain LPMO9H: Low-resolution SAXS model and synergy with cellulases

Autor(es)

Higasi, Paula M. R. ^[1] ; Velasco, Josman A. ^[2] ; Pellegrini, Vanessa O. A. ^[1] ; de Araujo, Evandro A. ^[1] ; Franca, Bruno Alves ^[2] ; Keller, Malene B. ^[3] ; Labate, Carlos A. ^[4] ; Blossom, Benedikt M. ^[3] ; Segato, Fernando ^[2] ; Polikarpov, Igor ^[1]

Afiliação do(s) autor(es)

^[1] Univ Sao Paulo, Sao Carlos Inst Phys, Av Trabalhador Sao Carlense 400, Sao Carlos, SP - Brazil

^[2] Univ Sao Paulo, Lorena Sch Engn, Estr Municipal Campinho S-N, Lorena, SP - Brazil

^[3] Univ Copenhagen, Dept Geosci & Nat Resource Management, Rolighedsvej 23, DK-1958 Frederiksberg C - Denmark

^[4] Univ Sao Paulo, Luiz de Queiroz Coll Agr, Av Padua Dias 11, Piracicaba, SP - Brazil

• Tipo de documento: Artigo Científico
• Fonte: Carbohydrate Polymers; v. 260, MAY 15 2021.
• Citações Web of Science: 0

Resumo

Lytic polysaccharide monooxygenases (LPMOs), monocopper enzymes that oxidatively cleave recalcitrant polysaccharides, have important biotechnological applications. Thermothelomyces thermophilus is a rich source of biomass-active enzymes, including many members from auxiliary activities family 9 LPMOs. Here, we report biochemical and structural characterization of recombinant TtLPMO9H which oxidizes cellulose at the C1 and C4 positions and shows enhanced activity in light-driven catalysis assays. TtLPMO9H also shows activity against xyloglucan. The addition of TtLPMO9H to endoglucanases from four different glucoside hydrolase families (GH5, GH12, GH45 and GH7) revealed that the product formation was remarkably increased when TtLPMO9H was combined with GH7 endoglucanase. Finally, we determind the first low resolution small-angle X-ray scattering model of the two-domain TtLPMO9H in solution that shows relative positions of its two functional domains and a conformation of the linker peptide, which can be relevant for the catalytic oxidation of cellulose and xyloglucan. (AU)

• Processo FAPESP: 15/13684-0 - Estudos estruturais e funcionais de enzimas que participam na síntese e degradação de carboidratos complexos
• Beneficiário: Igor Polikarpov
• Modalidade de apoio: Auxílio à Pesquisa - Temático
• Processo FAPESP: 17/01165-4 - Enzimas e eletrons ao trabalho: duplo processamento de carboidratos e lignina produzindo oligossacarídeos probióticos e ligninas bioativas
• Beneficiário: Carlos Alberto Labate
• Modalidade de apoio: Auxílio à Pesquisa - Regular