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Preparation and characterization of cross linked enzyme aggregates (CLEAs) of Bacillus amyloliquefaciens alpha amylase

Author(s): Sachin Talekar | Sailee Waingade | Vishal Gaikwad | Sucheta Patil | Nupur Nagavekar

Journal: Journal of Biochemical Technology
ISSN 0974-2328

Volume: 3;
Issue: 4;
Start page: 349;
Date: 2012;
Original page

Keywords: Enzyme immobilization | cross linked enzyme aggregates | carrier free | alpha amylase | ammonium sulfate | glutaraldehyde

Stabilization of enzymes is one of the major challenges in biocatalytic processes. Alpha amylase from Bacillus amyloliquefaciens was immobilized as a cross-linked enzyme aggregates (CLEAs). Alpha amylase was aggregated using ammonium sulfate. The resultant aggregates on cross-linking with glutaraldehyde produced insoluble catalytically active cross-linked enzyme aggregates. The effects of precipitation and cross-linking were studied and immobilized alpha amylase was characterized. 70% ammonium sulfate saturation, 2 %( v/v) glutaraldehyde, were used; 6 h cross-linking reaction at room temperature was performed and 100% activity recovery was achieved in CLEAs with enhanced thermal and acidic condition stabilities. The cross-linked enzyme aggregates exhibited pH optima of 6.0 and higher temperature optima of 60°C. Although after immobilization maximum velocity of enzyme reaction did not change, substrate affinity of the enzyme increased. Alpha amylase CLEAs retained 65% activity after 4 reuses with 30 min of each reaction time. The Scanning electron microscopy analysis showed that morphology of CLEAs substantially changed after 4 reuses.
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