Abstract:

Ksilanaz, which washes the β-1.4 glycosidal bonds of ksilan, which consists of β-1,4-linked xylopiranazyl residues, is an industrial enzyme with extensive potential applications in the textile, food, oven and biofuel industries, primarily paper and paper powder industries. In this study, the Kilis 7 December University center campus land sample is studied by the isolation of bacillus spp sulfur from the bacillus producer and the applicability of purified bacillus in various industries. The liquid fermentation environment containing ksilana is developed from the bacillus spp juice to the cell-free raw ksilanaz preparation is purified by applying ammonium sulfate and alcohol breakdown. The highest total and specific enzyme activity was found in the raw enzyme preparation at 723 U/L and 64.81 U/mg. The optimum activity of xylanaz is determined at 90°C and pH 10.6. The activity of the enzyme after 15 minutes of pre-incubation at a temperature of 90°C increased by up to 167%. The highest activity in characterization studies is estimated at 2935 U/L. In SDS-PAGE and zimogram analysis, a single protein band with an average molecular weight of 38.75 kDa of partially purified extracellular ksilanaza was observed. Xylos and xylosaccharides are determined as break-off products as a result of hydrolysis by xylanase enzyme and hydrolysis.

Keywords:

Abstract:

Xylanase that cleaves β-1,4-glycosidic linkages of xylan composed of β-1,4-linked xylopyranosyl residues, is a industrial enzyme, have widespread potential applications in the textile, feed, beverage and biofuel industries, especially the paper and pulp industry. In this study, we were examined to the isolation of Bacillus spp strains, produced extracellular xylanase, from Kilis 7 Aralık University central campus soil sample and the application in various industries of purificated xylanase. The cell-free crude xylanase preparate obtained from Bacillus spp strain developed in a liquid fermentation medium including xylan was purified by using ammonium sulfate and alcohol precipitation. The highest total and specific enzyme activities were detected as 723 U/L and 64.81 U/mg in cell-free crude xylanase preparate. The optimum activity of xylanase was emerged at 90°C and pH 10.6. After the pre-incubation of enzyme at 90°C for 15 min, its activity was detected to increase up to 167%. In characterization studies, the highest enzyme activity was calculated as 2935 U/L. In SDS-PAGE and zymogram analysis, single protein band in 38.75 kDa molecular weight belonging to the partially purified extracellular xylanase was observed. Xylose and xylo-oligosaccharides were detected as the products by hydrolysis of xylan with xylanase.