Endo-β-1,4-xylanases (EC 3.2.1.8) are able to hydrolyse xylan, the second most abundant polysaccharide in plant cell walls. In this work, two recombinant xylanases derived from Orpinomyces xynA gene were studied: one with mutations A226T and V135A (XM) and the other without mutations (XNM). They have been cloned in E. coli/pET24b, using IPTG as inducer and purified using ion exchange chromatography (Q-Sepharose). After purification, only one band of 25 kDa, corresponding to xylanases, was visualized on SDS-PAGE. Specific activities and Km against arabinoxylan were 12.844 U.mg -1 and 0.0021 mg.mL -1 for XNM and 10.794 U.mg -1 and 0.0014 mg.mL -1 for XM. The mutations improve thermo stability. The half-life of XNM was 220 min and 31 min at 50 °C and 60 °C, while for XM the values were 440 and 71 min at 50 o C and 60 o C, respectively. The clarification assays were conducted at 60 o C, 100 rpm for 60 min, using 50U xylanase/mL apple juice. The parameters available was pH, A660 (clarity), L* (luminosity), C (chroma) and h* (hue). All the juices tended to orange while only enzymatically treated with XM had an increase in color intensity (chroma / C) and higher content of soluble solids (sst) of 4,7 o brix. The results indicate that the processing of apple juice with xylanases can promote clarification and improvement of its properties.