Heterologous expression of a new lytic polysaccharide monooxygenase from Hahella ganghwensis and their functional characterization.

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.

Bibliographic Details

Main Authors:	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.
Other Authors:	Lucas F. Gregorine; Antonielle V. Monclaro; Caio de Oliveira Gorgulho Silva, Consultor da Embrapa Agroenergia; Kelly B. Rodrigues; Jéssica S. G. Peixoto, UnB; PATRICIA VERARDI ABDELNUR, CNPAE; LEIA CECILIA DE LIMA FAVARO, CNPAE.
Format:	Separatas biblioteca
Language:	English eng
Published:	2019-09-23
Subjects:	Spectrometric, Chromatographic,
Online Access:	http://www.alice.cnptia.embrapa.br/alice/handle/doc/1112393
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