Limit dextrinase (EC 3•2•1•41) partially purified from rice seeds was immobilized by adsorption on γ-alumina beads. Binding and activity yields were 88 and 52%, respectively. The adsorbed enzyme showed a broader pH optimum and an increased thermal stability compared to the free one. Optimum temperature was between 50 and 60°C and the enzyme retained about 70% of the initial activity after 7 days of incubation at 40°C in the presence of Ca2+. The immobilized biocatalyst degraded pullulan completely to maltotriose and effectively converted both acid hydrolysed amylodextrins and β-limit dextrins into maltose and maltotriose.
Immobilisation of rice limit dextrinase on gamma-alumina beads and its possible use in starch processing
CURIONI, ANDREA
1997
Abstract
Limit dextrinase (EC 3•2•1•41) partially purified from rice seeds was immobilized by adsorption on γ-alumina beads. Binding and activity yields were 88 and 52%, respectively. The adsorbed enzyme showed a broader pH optimum and an increased thermal stability compared to the free one. Optimum temperature was between 50 and 60°C and the enzyme retained about 70% of the initial activity after 7 days of incubation at 40°C in the presence of Ca2+. The immobilized biocatalyst degraded pullulan completely to maltotriose and effectively converted both acid hydrolysed amylodextrins and β-limit dextrins into maltose and maltotriose.File in questo prodotto:
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