In vitro and in silico characterization of metagenomic soil-derived cellulases capable of hydrolyzing oil palm empty fruit bunch

•Identification of cellulases in metagenomic clones.•Characterization of the cellulases’ activity on oil palm empty fruit bunch.•Use of homology modeling and molecular docking to characterize the enzymes. Diversification of raw material for biofuel production is of interest to both academia and indu...

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Published in:Biotechnology reports (Amsterdam, Netherlands) Netherlands), 2017-09, Vol.15 (C), p.55-62
Main Authors: Medina, Laura Marcela Palma, Ardila, Diana Catalina, Zambrano, María Mercedes, Restrepo, Silvia, Barrios, Andrés Fernando González
Format: Article
Language:English
Subjects:
beta-glucosidase
biofuels
biotechnology
byproducts
Cellulases
DNA
Elaeis guineensis
fats and oils industry
forest ecosystems
Fractal-like kinetic model
fuel production
genomic libraries
kinetics
lignocellulose
mass transfer
Metagenomics
Molecular docking
molecular models
Oil palm empty fruit bunch
raw materials
sequence analysis
temperature
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Summary:•Identification of cellulases in metagenomic clones.•Characterization of the cellulases’ activity on oil palm empty fruit bunch.•Use of homology modeling and molecular docking to characterize the enzymes. Diversification of raw material for biofuel production is of interest to both academia and industry. One attractive substrate is a renewable lignocellulosic material such as oil palm (Elaeis guineensis Jacq.) empty fruit bunch (OPEFB), which is a byproduct of the palm oil industry. This study aimed to characterize cellulases active against this substrate. Cellulases with activity against OPEFB were identified from a metagenomic library obtained from DNA extracted from a high-Andean forest ecosystem. Our findings show that the highest cellulolytic activities were obtained at pH and temperature ranges of 4–10 and 30°C–60°C, respectively. Due to the heterogeneous character of the system, degradation profiles were fitted to a fractal-like kinetic model, evidencing transport mass transfer limitations. The sequence analysis of the metagenomic library inserts revealed three glycosyl hydrolase families. Finally, molecular docking simulations of the cellulases were carried out corroborating possible exoglucanase and β-glucosidase activity.
ISSN:2215-017X
2215-017X
DOI:10.1016/j.btre.2017.06.003