Production of xylo-oligosaccharides by immobilized-stabilized derivatives of endo-xylanase from Streptomyces halstedii

► An endoxylanase from Streptomyces halstedii was stabilized by multipoint covalent immobilization on glyoxyl-agarose supports. ► The immobilized enzyme derivatives preserved 65% of their catalytic activity and were 200 times more stable than the soluble enzyme. ► The rate and yield of enzymatic hydrolysis of xylan were greatly improved at high temperatures. ► After 80% of enzymatic hydrolysis an mixture of small xylo-oligosaccharides was obtained. 50% of xylan was converted in XOS. ► The immobilized derivative was highly stable under optimal experimental conditions.