This study evaluates various immobilization methods for α-amylase, highlighting sodium alginate's effectiveness in enhancing stability and reusability.
Enzyme immobilization enhances stability, performance, and reusability for various applications. The present study evaluated various immobilization methods for α-amylase from Aspergillus tamarii MTCC5152, including ionic exchange, physical adsorption, and entrapment. Among the tested matrices, sodium alginate was most effective, retaining 74% activity. The immobilized enzyme retained 45% of its original activity even after being reused for 7 cycles. Optimal performance was observed at pH 6.5 in Tris-HCl buffer, with 2% alginate and 3% calcium chloride, with activity influenced by enzyme concentration, reaction time, and matrix rigidity. Compared to other methods, alginate entrapment minimized enzyme leakage and improved enzymatic activity, highlighting its potential for industrial use, especially in the leather sector. Comprehensive surface and structural analysis to clarify enzyme-matrix interactions and kinetic studies of immobilized enzymes will be the main emphasis of further investigations.
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Arunachallam et al. (2025) studied this question.
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