Study of structural and molecular interaction for the catalytic activity of cellulases: An insight in cellulose hydrolysis for higher bioethanol yield

Publication date: 15 March 2020Source: Journal of Molecular Structure, Volume 1204Author(s): Manish Paul, Gayatree Panda, Pradeep Kumar Das Mohapatra, Hrudayanath ThatoiAbstractComparative sequence alignment, molecular modeling and docking analyses were performed taking 5 microbial (3 bacteria and 2 fungi) cellulase enzymes and its substrate β-D glucose in order to understand the enzyme-substrate interaction and binding affinity associated with cellulose hydrolysis. Amino acids such as Val114, Ala255, Val288, Val289, and Ser301 of Streptomyces sp. Endoglucanase-1 shown to bind with β-D glucose. The binding energy between the modeled cellulase and substrate complex resulted that Endoglucanase-1 from Streptomyces sp. has the most binding affinity of −5.61 kcal/mol for the cellulose unit. Deleterious mutations in cellulase enzyme, E133A and H98A reported previously in Dickeya dadantii have been designed and validated using in silico approach. The number of hydrogen bond interactions reported in wild type Endoglucanase-1 from Streptomyces sp. was 22, whereas E133A and H98A mutant cellulase from Dickeya dadantii, the interaction number comes down to 5 and 6 respectively. Binding energy recorded for these two mutants is −4.52 and −4.91 respectively which is less than its wild type form. Phylogenetic tree analysis suggests that the modeled cellulase enzyme from Streptomyces sp. is closely related to the cellulase from Thermobispora bispora, Cellulomonas fimi, Streptomyce...
Source: Journal of Molecular Structure - Category: Molecular Biology Source Type: research