Optimization and Biochemical Characterization of Thermo-Alkalotolerant Cellulase Enzyme From Aspergillus Terreus PPCF

Abstract

The aim of this study was to boost the production rate of a novel thermo-alkalotolerant cellulase (FPase) enzyme from the fungal isolate Aspergillus terreus PPCF. Initially, the extracellular FPase activity was 0.166 ± 0.03 UmL-1 in the culture filtrate, which further increased up to 0.91 ± 0.13 UmL-1 under optimized conditions (3% w/v wheat bran and 0.5% w/v ammonium sulfate). Through response surface methodology, the FPase activity was enhanced to 10.78 UmL1 under the cumulative effect of different factors. The zymogram analysis revealed only one activity band, with the molecular weight of ~110 KDa. The optimum pH was 7.0, but the enzyme was stable in a pH range of 4-10. The optimum temperature was 50 °C, but the stability range of the enzyme was 30-90 °C. The maximum effect of Mg2+ was observed on the FPase enzyme. The findings of the present study demonstrate the thermo- and alkalotolerance of the obtained cellulase enzyme, which will be beneficial to the biofuel and other industries.

Optimization of substrate composition for pectinase production from Satkara (Citrus macroptera) peel using Aspergillus niger-ATCC 1640 in solid-state fermentation

“…[ 48 ] and Parveen et al. [ 49 ] showed the significant effect of ZnSO 4 as a metal ion on the activity of inulinase and cellulase enzyme, respectively. The same trend was also recorded in the case of MgSO 4 .7H 2 O.…”