Immobilization of xylanase from Thermomyces lanuginosus SSBP using Eudragit S-100
XYLANASE FROM A LOCALLY ISOLATED fungus, T. lanuginosus SSBP, was immobilized on the polymers alginate, chitosan, and Eudragit S-100. The activity of the precipitated enzyme was greatest on the last and so all further tests were conducted on this substrate. Xylanase was non-covalently bound to Eudragit S-100, and showed greater thermal stability than the free enzyme at 70°C; no change was observed at the pH optimum (6.5) of the immobilized enzyme. Moreover, the xylanase retained 62% of its activity after six precipitation cycles on the polymer matrix. The enhanced characteristics of xylanase after immobilization may be useful for the bleaching of pulp in the pulp and paper industry. We believe that this is the first report on the use of polymer matrices to bind xylanase from a thermophilic T. lanuginosus strain.