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Enzyme Research
Volume 2011, Article ID 483943, 4 pages
Research Article

Activated Charcoal—A Potential Material in Glucoamylase Recovery

1Department of Microbiology, University of Agriculture, PMB 2240, Abeokuta, Nigeria
2Department of Food Science and Technology, University of Agriculture, PMB 2240, Abeokuta, Nigeria

Received 28 April 2011; Revised 20 September 2011; Accepted 21 September 2011

Academic Editor: J. Guisan

Copyright © 2011 S. O. Kareem et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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.