Refining process and properties of polysaccharide xylanase

Abstract

The xylanase enzyme with a specific activity of 5676.4 units/mg of protein and a purification degree of 53.1 was isolated and purified from the complex enzyme preparation Brusiem BGX. The enzyme was isolated by ethanol precipitation, and purification was performed by gel filtration on sefadex G-25 and G-150 and ion exchange chromatography on DEAE-cellulose. The effect of temperature and pH on the activity and stability of the enzyme in the temperature range of 30-70 °C and pH 4.0-7.0 was studied. The optimum action of xylanase is a pH of 5.5 and a temperature of 50 °C. The enzyme has a sufficiently high thermal and acid stability, hydrolyzes non-starchy polysaccharides containing (1,4) - β-D-xyloside bonds. In this regard, its use in biotechnology for hydrolysis of non-starchy polysaccharides of grain in the brewing and in the production of ethanol is prospectively.