01787nam a2200205 a 450000100080000000500110000800800410001910000210006024501590008126002030024052009700044365300200141365300180143370000200145170000230147170000210149470000220151570000200153770000240155721123932019-09-23       2019    bl uuuu     u00u1 u    #d1 aGREGORINE, L. F.  aHeterologous expression of a new lytic polysaccharide monooxygenase from Hahella ganghwensis and their functional characterization.h[electronic resource]  aIn: SIMPÓSIO NACIONAL DE BIOPROCESSOS, 22.; SIMPÓSIO DE HIDRÓLISE ENZIMÁTICA DE BIOMASSA, 13., 2019, Uberlandia, MG. [Anais ...]. São Paulo: Associação Brasileira de Engenharia Químicac2019  aThe 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.  aChromatographic  aSpectrometric1 aMONCLARO, A. V.1 aSILVA, C. de O. G.1 aRODRIGUES, K. B.1 aPEIXOTO, J. S. G.1 aABDELNUR, P. V.1 aFAVARO, L. C. de L.