Production, Partial Purification and Some Properties of α-L-Arabinofuranosidase from Chaetomium thermophile and Talaromyces thermophilus

THE PRODUCTION of extracellular α-L-arabinofuranosidase (ABFase), partial purification and some of its properties by locally isolated strains of Chaetomium thermophile and Talaromyces thermophilus were studied. The best static culture conditions for the enzyme production were 2% sugar beet pulp; pH 5.0 and 45ºC for both strains. The best nitrogen source is ammonium sulphate for C. thermophile and yeast extract for T. thermophilus. The enzyme was partially purified from the culture supernatant by precipitation with ammonium sulfate treatment, gel filtration on Sephadex G100, with purification fold 15.89 and 8.32 for C. thermophile and T. thermophilus, respectively. The purified enzyme of both fungi displayed an optimal activity at 50 ºC. The enzyme was stable at temperatures between 30-70 ºC. The optimum pH for C. thermophile was 5.5 and the enzyme was stable at pH between 3.0 – 6.5. While the optimum pH for T. thermophilus was 6.5 and the enzyme was stable at pH between 3.0 – 7.5.