An acidothermophilic functionally active novel GH12 family endoglucanase from Aspergillus niger HO: purification, characterization and molecular interaction studies.

Endoglucanase (EG) from Aspergillus niger HO was sequentially purified through ultrafiltration, ion exchange and size exclusion chromatography to homogeneity, with an overall recovery of 18 %. The purified EG was a monomeric protein with a molecular weight of about 55 kDa. The enzyme was optimally active at pH 3.

Effect of nickel-cobaltite nanoparticles on production and thermostability of cellulases from newly isolated thermotolerant Aspergillus fumigatus NS (class: Eurotiomycetes).

In the present study, effect of nickel-cobaltite (NiCo2O4) nanoparticles (NPs) was investigated on production and thermostability of the cellulase enzyme system using newly isolated thermotolerant Aspergillus fumigatus NS belonging to the class Euratiomycetes. The NiCo2O4 NPs were synthesized via hydrothermal method assisted by post-annealing treatment and characterized through X-ray diffraction (XRD) and transmission electron microscopy (TEM) techniques. In the absence of NPs in the growth medium, filter paper cellulase (FP) activity of 18 IU/gds was achieved after 96 h, whereas 40 % higher FP activity in 72 h was observed with the addition of 1 mM concentration of NPs in the growth medium.

Response surface optimization for enhanced production of cellulases with improved functional characteristics by newly isolated Aspergillus niger HN-2.

Fungi isolated from partially decayed wood log samples showing characteristic diversity for spore colour, colony morphology and arrangement of spores were assessed for cellulolytic enzyme production. Isolates showing a cellulolytic index of ≥2.0 were assayed for filter paper (FP) cellulase and β-glucosidase (BGL) production.

Purification and characterization of an acidothermophilic cellulase enzyme produced by Bacillus subtilis strain LFS3.

In the present investigation, a microorganism hydrolyzing carboxymethylcellulose (CMC) was isolated and identified as Bacillus subtilis strain LFS3 by 16S rDNA sequence analysis. The carboxymethylcellulase (CMCase) enzyme produced by the B. subtilis strain LFS3 was purified by (NH₄)₂SO₄ precipitation, ion exchange and gel filtration chromatography, with an overall recovery of 15 %.

Effect of abiotic stress on phosphate solubilization by biocontrol fungus Trichoderma sp.

This study was undertaken to explore the role of Trichoderma sp. in phosphate (P) solubilization and antagonism against fungal phytopathogens. All fungal isolates (SE(6), KT(6), KT(28), and BRT(11)) and a standard culture of T.