Author(s)

Marília Lordêlo Cardoso Silva¹, Volnei Brito de Souza¹, Verônica da Silva Santos¹, Hélio Mitoshi Kamida², João Ronaldo T. de Vasconcellos-Neto², Aristóteles Góes-Neto², Maria Gabriela Bello Koblitz^3*

¹Technology Department, State University of Feira de Santana (UEFS), Feira de Santana, Brasil.
²Biology Department, State University of Feira de Santana (UEFS), Feira de Santana, Brasil.
³Food Technology Department, Federal University of the State of Rio de Janeiro (UNIRIO), Rio de Janeiro, Brasil.

Manganese peroxidase (MnP) is a ligninolytic enzyme that is involved in the removal of lignin from the cell wall of plants. This removal facilitates the access of hydrolytic enzymes to the carbohydrate polymers that are hydrolyzed to simple sugars, which allows the subsequent fermentation to obtain bioproducts, such as ethanol. In this work, response surface methodology (RSM) was employed to optimize the culture conditions on unexpensive substrate for MnP secretion by Trametes villosa. Three independent variables were evaluated (i.e., temperature, moisture content and pH). The crude extract containing MnP was used in the delignification experiment and it caused a reduction in lignin content for all residues tested: 35.05 ± 1.45 (%) for the sugar cane bagasse; 63.11 ± 0.06 (%) for the sisal fiber and 39.61 ± 0.39 (%) for the coconut shell, under the reaction conditions tested after 4 hours of fermentation. The preliminary results exhibited the potential application of this enzyme in the removal of lignin from plant residues. However, the conditions should be evaluated and optimized for each residue type.

Ligninolytic Enzymes, Basidiomycete, Sugarcane Bagasse, Coconut Shell, Sisal Fiber

Silva, M. , Souza, V. , Santos, V. , Kamida, H. , Vasconcellos-Neto, J. , Góes-Neto, A. and Bello Koblitz, M. (2014) Production of Manganese Peroxidase by Trametes villosa on Unexpensive Substrate and Its Application in the Removal of Lignin from Agricultural Wastes. Advances in Bioscience and Biotechnology, 5, 1067-1077. doi: 10.4236/abb.2014.514122.