The primary plant cell wall is composed of cellulose, hemicellulose, lignin and protein in a stable matrix. The concomitant depolymerization of lignin by laccase and of hemicelluloses by xylanase can improve lignocellulose degradation in the production of second generation biofuels. A thermophilic variant of xylanase A (XynAG3) and the thermostable laccase (CotA), both from Bacillus subtilis, were produced in co-transformed Pichia pastoris strain GS115. Mobility changes in SDS-PAGE after Endo H digestion indicated that both enzymes were glycosylated. The maximum catalytic activity of the XynAG3<SUB>Pp</SUB> and the CotA<SUB>Pp</SUB> was observed at 58<SUP>o</SUP>C and 75<SUP>o</SUP>C, respectively, and both enzymes presented high activity at pH 5.0. The half-life at 60<SUP>o</SUP>C of XynAG3<SUB>Pp</SUB> and CotA<SUB>Pp</SUB> was 150min and 540min, respectively. The relative levels of CotA<SUB>Pp</SUB> and XynAG3<SUB>Pp</SUB> in culture broths were altered by the concentration of methanol used for induction, and CotA<SUB>Pp</SUB>:XynAG3<SUB>Pp</SUB> ratios of 1:1.5 and 1:2 were evaluated against milled sugar-cane bagasse. The highest activity was observed at a 1:2 ratio of CotA<SUB>Pp</SUB>:XynAG3<SUB>Pp</SUB>, and was 44% higher as compared to the sum of the activities of the individual enzymes in the same assay conditions. These results demonstrate the synergistic action between an endoxylanase and a laccase against the natural lignocellulosic substrate.