Abstract
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.
Highlights
Enzyme purification is a necessary prerequisite for a full understanding of the nature and mechanism of action of the enzyme [1]
The use of carboxy-methyl cellulose, tannic acid, and edible gum as precipitants and as well as organic solvents poses the problem of product recovery [5, 6]
This study reports application of activated charcoal in the recovery of fungal amylases
Summary
Enzyme purification is a necessary prerequisite for a full understanding of the nature and mechanism of action of the enzyme [1]. Activated charcoal is an adsorbent widely used in the treatment of wastewater and industrial contaminants by virtue of its high removal capacity and adaptability for a wide range of pollutants [8]. It is made from any essentially carbonaceous materials. Activated charcoal is used to remove compounds that cause objectionable taste, colour, and odour in water treatment while its industrial applications involve removal of toxic gases and pesticides and as well as purification of organic compounds [10, 11]. This study reports application of activated charcoal in the recovery of fungal amylases
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