Chemical and Process Engineering Research
Purification and Characterization of Invertase from Aspergillus terreus
Abstract
Invertase was produced from Aspergillus terreus under optimized culture conditions at six days of incubation with pH 7.0 and 25°C, in Czapek Dox media by solid state fermentation (SSF). The enzyme was partially purified by dialysis followed by DEAE-column chromatography. Purification fold and enzyme yield, while stabled at 20-40°C with pH 3.0-5.0. The activation energy for substrate conversion was 1.87Kcal/mol. Thin layer chromatography (TLC) shown that glucose and fructose were the products of sucrose hydrolysis. The partial purified enzyme was immobilized with different metals, while Fe+3 gave highest activity with residual activity 76.52%. Storage activity for immobilized enzyme at 4°C after 2 and 4 weeks were 70.94 % and 58.42% respectively.
Key words: Invertase, Purification, Immobilization
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ISSN (Paper)2224-7467 ISSN (Online)2225-0913
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