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Upscale and characterization of lignin-modifying enzymes from Marasmiellus palmivorus VE111 in a bioreactor under parameter optimization and the effect of inducers
- Schneider, William Daniel Hahn, Costa, Paula Cavion, Fontana, Roselei Claudete, de Siqueira, Félix Gonçalves, Pinheiro Dillon, Aldo José, Camassola, Marli
- Journal of biotechnology 2019 v.295 pp. 1-8
- Marasmiellus, bioreactors, copper, copper sulfate, enzyme activity, laccase, manganese, manganese peroxidase, manganese sulfate, oxygen, pH, temperature
- Testing different pHs, dissolved oxygen concentrations and temperatures, plus the addition of inducers, to optimize ligninolytic enzyme activity, resulted in increased production of laccases, total peroxidases and manganese peroxidases on the order of 2.1-fold, 4.6-fold and 10-fold, respectively; laccases reached 6588 U/mL, total peroxidases reached 3533 U/mL and manganese peroxidase achieved 60 U/mL. Furthermore, an increase in laccase volumetric productivity and in its specific activity was verified. The addition of inducers, such as copper sulphate and manganese sulphate, improved enzymatic activity. In addition, a new previously unidentified laccase isoform was documented by zymography. The present work successfully increased the production of ligninolytic enzymes.