Molecular dynamics-based structural insights of the first putative endoglucanase, PsGH5A of glycoside hydrolase family 5 from Pseudopedobacter saltans.

Context: The putative endoglucanase, PsGH5A, from Pseudopedobacter saltans of family GH5 contains a catalytic module, PsGH5 (β/α)-TIM barrel), at N-terminal followed by a family 6 carbohydrate-binding module (CBM6, β-sandwich). Superposition of PsGH5A with PDB homologs revealed Glu220 and Glu318 as evolutionarily conserved and catalytic residues performing the hydrolysis through retaining-type mechanism, a canonical property of GH5 family. PsGH5A showed higher affinity for longer cellooligosaccharides, as long as cellodecaose with binding free energy (∆G) of - 13.

Computational design and structure dynamics analysis of bifunctional chimera of endoxylanase from and xylosidase from .

Development of chimeric enzymes by protein engineering can more efficiently contribute toward biomass conversion for bioenergy generation. Therefore, prior to experimental validation, a computational approach by modeling and molecular dynamic simulation can assess the structural and functional behavior of chimeric enzymes. In this study, a bifunctional chimera, Xyn11A-GH43A comprising an efficient endoxylanase (Xyn11A) from and xylosidase (GH43A) from was computationally designed and its binding and stability analysis with xylooligosaccharides were performed.

Multifunctionality and mechanism of processivity of family GH5 endoglucanase, RfGH5_4 from Ruminococcus flavefaciens on lignocellulosic polymers.

Multifunctional endoglucanase, RfGH5_4 from Ruminococcus flavefaciens showed (β/α)-TIM barrel structure by homology modeling. Glu168 and Glu292 residues acted as general acid and base during catalysis. Circular Dichroism results, 40.

Optimization and biochemical characterization of a thermotolerant processive cellulase, PtCel1, of Parageobacillus thermoglucosidasius NBCB1.

Vermicomposting involves enrichment of microorganisms that are able to resist higher temperatures and perform simultaneous degradation of lignocellulose, and therefore, such microbial communities are a potential source of cellulolytic enzymes. This study aimed to optimize the production of a processive cellulase by Parageobacillus thermoglucosidasius NBCB1 isolated from vermicompost, under submerged fermentation of rice straw and to characterize the purified enzyme for industrial suitability. Cellulase production in basal medium (7.

Highly efficient, processive and multifunctional recombinant endoglucanase RfGH5_4 from Ruminococcus flavefaciens FD-1 v3 for recycling lignocellulosic plant biomasses.

Gene encoding endoglucanase, RfGH5_4 from R. flavefaciens FD-1 v3 was cloned, expressed in Escherichia coli BL21(DE3) cells and purified. RfGH5_4 showed molecular size 41 kDa and maximum activity at pH 5.

Functional characterization of thermotolerant microbial consortium for lignocellulolytic enzymes with central role of Firmicutes in rice straw depolymerization.

Rice (Oryza sativa L.) straw, an agricultural waste of high yield, is a sustainable source of fermentable sugars for biofuel and other chemicals. However, it shows recalcitrance to microbial catalysed depolymerization.