Production of thermostable β-glucosidase and CMCase by Penicillium sp. LMI01 isolated from the Amazon region

• Published in: Electronic Journal of Biotechnology 2018-01, Vol.31 (1), p.84-92
• Main Authors: Santa-Rosa, Pamella S, Souza, Anita L, Roque, Rosemary A, Andrade, Edmar V, Astolfi-Filho, Spartaco, Mota, Adolfo J, Nunes-Silva, Carlos G
• Format: Article
• Language: English
• Subjects: Biocatalysts; Cellulases; Cellulose hydrolysis; Endoglucanase; Exoglucanase; Hydrolysis of lignocellulose; Internal transcribed spacer; Microbial cellulolytic enzymes; Oligosaccharides; Submerged fermentation; Trichoderma reesei
• ISSN: 0717-3458; 0717-3458
• DOI: 10.1016/j.ejbt.2017.11.005

Background: Cellulolytic enzymes of microbial origin have great industrial importance because of their wide application in various industrial sectors. Fungi are considered the most efficient producers of these enzymes. Bioprospecting survey to identify fungal sources of biomass-hydrolyzing enzymes from a high-diversity environment is an important approach to discover interesting strains for bioprocess uses. In this study, we evaluated the production of endoglucanase (CMCase) and β-glucosidase, enzymes from the lignocellulolytic complex, produced by a native fungus. Penicillium sp. LMI01 was isolated from decaying plant material in the Amazon region, and its performance was compared with that of the standard isolate Trichoderma reesei QM9414 under submerged fermentation conditions. Results: The effectiveness of LMI01was similar to that of QM9414 in volumetric enzymeactivity (U/mL); however, the specific enzyme activity (U/mg) of the former was higher, corresponding to 24.170 U/mg of CMCase and 1.345 U/mg of β-glucosidase. The enzymes produced by LMI01 had the following physicochemical properties: CMCase activity was optimal at pH 4.2 and the β-glucosidase activity was optimal at pH 6.0. Both CMCase and β-glucosidase had an optimum temperature at 60°C and were thermostable between 50 and 60°C. The electrophoretic profile of the proteins secreted by LMI01 indicated that this isolate produced at least two enzymes with CMCase activity, with approximate molecular masses of 50 and 35 kDa, and β-glucosidases with molecular masses between 70 and 100 kDa. Conclusions: The effectiveness and characteristics of these enzymes indicate that LMI01 can be an alternative for the hydrolysis of lignocellulosic materials and should be tested in commercial formulations.