期刊
ENZYME AND MICROBIAL TECHNOLOGY
卷 109, 期 -, 页码 25-30出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.enzmictec.2017.09.007
关键词
Enzyme; Laccase; Phenols; Deactivation; Activation
资金
- Fundacao de Amparo a Pesquisa do Estado de Minas Gerais (FAPEMIG)
- Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES)
- Conselho Nacional de Pesquisa e Desenvolvimento Tecnologico (CNPq)
- Purdue University Agricultural Research Programs [10677, 10646]
- Department of Agricultural and Biological Engineering
- CAPES, Brazil [000218/2014-06, 012981/2013-03]
Cellulase and hemicellulase activities in a 1:1 ratio of enzymes extracted from Chrysoporthe cubensis and Penicillium pinophilum were evaluated in the presence of known monocomponent phenolic inhibitors and also with phenol mixtures derived from alkali pretreated sugarcane bagasse. The cellulolytic activities from C. cubensis:P. pinophilum displayed a much higher tolerance to phenolic inhibitors than equivalent enzyme activities obtained from Tnchodennareesei and Aspergillus niger. Enzymes from T. reesei and A. niger were deactivated at 0.3 and 1.5 mg phenols/mg protein, respectively, as reported previously, while enzymes from C. cubensis:P. pino-philum resisted deactivation at 35 mg phenols/mg protein. However, tolerance of xylanase with respect to phenols required the presence of laccase. Removal of laccase (enzyme) activity using sodium azide resulted in a 2x higher xylanase deactivation (from 40% to 80%). This paper identifies enzymes that are phenol tolerant, and whose adoption for lignocellulose hydrolysis could contribute to reductions in enzyme loading needed to hydrolyze alkali pretreated lignocellulosic substrates in the presence of lignin derived phenols.
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