Synergistic action of co-expressed xylanase/laccase mixtures against milled sugar cane bagasse |
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| Institution: | 1. Departamento de Bioquímica e Imunologia, FMRP-USP, Universidade de São Paulo, São Paulo, Brazil;2. Departamento de Química, FFCLRP-USP, Universidade de São Paulo, São Paulo, Brazil;3. Instituto de Química, Universidade Federal do Rio Grande do Norte – Natal, Rio Grande do Norte, Brazil;4. Institute for Research in Immunology and Cancer, Université de Montréal, Canada;5. Laboratório Nacional de Ciência e Tecnologia do Bioetanol – CTBE/CNPEM, Campinas, São Paulo, Brazil;1. Institute of Experimental Physics, SAS, Watsonova 47, 040 01 Kosice, Slovakia;2. Institute of Chemical Sciences, Faculty of Sciences, Safarik University, Kosice, Slovakia;3. Helmholtz-Zentrum Geesthacht: Centre for Materials and Coastal Research, Max-Planck-Street 1, 21502 Geesthacht, Germany;4. Joint Institute for Nuclear Research, Joliot-Curie 6, Dubna, 141980 Moscow Region, Russia;5. Kyiv Taras Shevchenko National University, Volodymyrska Street 64, Kyiv 01033, Ukraine;6. Department of Medical and Clinical Biochemistry and LABMED, Tr. SNP 1, 040 11 Kosice, Slovakia;1. Macrogen Inc., Gasan-dong, Seoul 153-781, Republic of Korea;2. Clean Energy Research Center, Korea Institute of Science and Technology (KIST), Seoul 136-791, Republic of Korea;3. Department of Chemical and Biomolecular Engineering, Sogang University, Seoul 121-742, Republic of Korea;4. Department of Molecular Science and Technology, Ajou University, Suwon 443-749, Republic of Korea |
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| Abstract: | 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 XynAG3Pp and the CotAPp was observed at 58 °C and 75 °C, respectively, and both enzymes presented high activity at pH 5.0. The half-life at 60 °C of XynAG3Pp and CotAPp was 150 min and 540 min, respectively. The relative levels of CotAPp and XynAG3Pp in culture broths were altered by the concentration of methanol used for induction, and CotAPp:XynAG3Pp 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 CotAPp:XynAG3Pp, 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. |
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| Keywords: | Xylanase A CotA Synergic activity Mass spectrometry |
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