Production, partial purification and some properties of alpha-L-arabinofuranosidase from chaetomium thermophile and talaromyces thermophius

ABSTRACT

The PRODUCTION of extracellular alpha-L-arabinofuranosidase [ABFase], partial purification and some of its properties by locally isolated strains of Chaetomiuin thermophile and Talaromyces therinophihis were studied. The best static culture conditions for the enzyme production were 2% sugar beet pulp; pH 5.0 and 45°C for both strains. The best nitrogen source is ammonium sulphate for C. thermophile and yeast extract for P thermophile us. The enzyme was partially purified from the culture supernatant by precipitation with ammonium sulfate treatment, gel filtration on Sephadex G[100]with purification fold 1589 and 8.32 for C. thermophile and T thermophilus, respectively. The purified enzyme of both fungi displayed an optimal activity at 50°C. The enzyme was stable at temperatures between 30-70°C. 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