The potential of activated charcoal in the purification of fungal glucoamylase was investigated. Various concentrations of activated charcoal (1-4% w/v) were used to concentrate crude glucoamylase from Rhizopus oligosporus at different temperature values (30-50°C). Effects of pH (3.0-6.0) and contact time (0-60 min) on enzyme purification were also monitored. Activated charcoal (3% w/v) gave a 16-fold purification in a single-step purification at 50°C for 20 min and pH 5.5. The result of SDS-PAGE analysis of purified glucoamylase showed two major protein bands with corresponding molecular weight of 36 kDa and 50 kDa. The method is inexpensive, rapid, and simple which could facilitate downstream processing of industrial enzyme.