Arachniotus citrinus, a fungal strain, was grown for 30 days at 30degree C, pH 6 under solid-state growth conditions on wheat bran ascarbon source for the production of glucoamylase (glucanoglucohydrolases). Specific activity of crude enzyme was 13.26 unitsmg-1. The enzyme was purified using Fast Protein LiquidChromatography (FPLC) unit and four-step purification procedure,comprised of ammonium sulfate precipitation, Hiload anion-exchange,hydrophobic interaction and Mono-Q anion-exchange chromatographywas used. The onset of glucoamylase precipitation occurred at 60% andcompleted at 75% saturation of ammonium sulfate at 0 degree C. Thepurification after ammonium sulfate precipitation was 2.48-fold and therecovery was 67%. While, recovery after Hiload chromatography was50% and their purity reached to about 20-fold. During hydrophobicinteraction chromatography (HIC) glucoamylase were eluted at 429 mMammonium sulfate and were 52-fold purified with respect to crude.The recovery of dialyzed glucoamylase after HIC was 33%.Glucoamylase after HIC were further purified to 63-fold on Mono-Qcolumn with a recovery of about 33% and their specific activity was839.1 U mg-' protein. The glucoamylase was monomeric in naturebecause its native molecular mass (87 kDa) determined on Gelfiltration, and the subunit mass (88 kDa) determined on 10% SDS-PAGEwere the same.