Autoria: GREGORINE, L. F.; MONCLARO, A. V.; SILVA, C. de O. G.; RODRIGUES, K. B.; PEIXOTO, J. S. G.; ABDELNUR, P. V.; FAVARO, L. C. de L.

Resumo: The powerful class of oxidative enzymes, lytic polysaccharide monooxygenases (LPMOs) - also named Auxiliary Activity (AA) - are able to oxidize recalcitrant polysaccharides on lignocellulosic biomass. In this work, we successfully expressed three catalytic domains from bacterial LPMOs in the yeast Komagataella phaffii: domain MdAA10.1-SD (from Moritella dasanensis), domain VmAA10.2-SD (from Verrucosispora maris), and domain HgAA10.1-SD (from Hahella ganghwensis). Heterologous expression was analyzed by SDS-PAGE, Western-Blot, and Dot-Blot, while functional activity of these proteins was investigated by a combination of mass spectrometric and chromatographic methods. The recombinant LPMO catalytic domain HgAA10.1-SD from H. ganghwensis, a C1-oxidizer, was able to promote an oxidative cleavage of phosphoric-acid swollen cellulose (PASC) substrate in the presence of ascorbic acid as an electron donor, showing its potential for cellulose depolymerization.

Ano de publicação: 2019

Tipo de publicação: Artigo em anais e proceedings

Unidade: Embrapa Agroenergia

Palavras-chave: Chromatographic, Spectrometric