Thermostability and Substrate Specificity of GH-11 Xylanase from Thermomyces lanuginosus VAPS24

Abstract

The three dimensional structure (3D structure) of GH-11 xylanase from was obtained through homology modeling. To study the enzyme interaction with an end product of enzyme catalysis, the xylanase two sugar molecules xylose and xylobiose has been docked into the active site of GH-11 xylanase through molecular docking. Based on the free binding energy and Inhibition constant, concluded xylose makes more stable complex than xylobiose. Further, the molecular dynamic simulation studies were carried out at different temperature, i.e. 323, 333, 343 and 353 K (i.e. 50, 60, 70 and 80 °C). It has been observed that there was minor structural modification in 3D-structure of xylanase at 323, 333, and 343 K. But the helix and sheets moved out of the initial structure when simulation carried out at during 353 K (80 °C).

Horseradish and potato peroxidase biobleaching of mixed office waste paper

“…To overcome the poor bleachability of MOW pulp by chemical agents, a wide number of enzymes, including cellulase (Tiwari et al 2018), xylanase (Kumar et al 2017), laccase (Riva 2006;Singh and Arya 2019), and peroxidase (Archibald 1992), have been studied (Biswas et al 2019b). The enzyme application in pulp and paper industry are limited due to their high cost, and it is hard to maintain their stability during the industrial process (Kumar et al 2018b(Kumar et al ,c, 2019aLin et al 2018). Synthetic dyes possess a complex structure, which requires high cost and high energy input during conventional biological wastewater treatment.…”