Title:	Heterologous expression of a new lytic polysaccharide monooxygenase from Hahella ganghwensis and their functional characterization.
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.
Affiliation:	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.
Date Issued:	2019
Citation:	In: SIMPÓSIO NACIONAL DE BIOPROCESSOS, 22.; SIMPÓSIO DE HIDRÓLISE ENZIMÁTICA DE BIOMASSA, 13., 2019, Uberlandia, MG. [Anais ...]. São Paulo: Associação Brasileira de Engenharia Química, 2019.
Description:	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.
Keywords:	Spectrometric Chromatographic
Type of Material:	Artigo em anais e proceedings
Access:	openAccess
Appears in Collections:	Artigo em anais de congresso (CNPAE)