The gene of a beta-xylanase (Tnap_0700) was cloned from a hyperthermophilic Thermotoga naphthophila strain ATCC BAA-489 and expressed in Escherichia coli BL21 (DE3) via pET-21a (+) as an expression vector. The growth steps were upgraded for highest beta-xylanase expression via several factors, for example, IPTG concentration, time of induction, pH, and temperature. The pH and temperature optima for the extreme expression of beta-xylanase were 7.0 pH and 37 degrees C, correspondingly. Recombinant enzyme purified by heat treatment process, then later by immobilized metal ion affinity chromatography. Molecular mass of the purified beta-xylanase was 38 kDa observed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme was stable at room temperature for 30 days. It exhibited high stability over wide series of temperature 50-90 degrees C and pH 4.0-9.0 upon the addition of 1 mM Ca+2 and reduced in the existence of Cu+2 and EDTA. The addition of about 10-30% different organic solvents have no considerable effect on enzyme. However, SDSF and urea acting as an inhibitor leads to decrease in the enzyme activity. The beta-xylanase enzyme was active to hydrolyze xylan from beechwood forming xylose. Thermostable beta-xylanase causes the breakdown of complex carbohydrates into monosaccharide components. This thermostable beta-xylanase revealed remarkable properties, which make it an encouraging candidate for various industrial applications especially in the alteration of renewable biomaterials into ethanol production, and biofuels from lignocellulosics has acknowledged much devotion subsequently in the last decade.