Enzyme immobilization on nanostructured substrates is an emerging method for the efficient development of nanobiocatalysts to enhance enzymatic performance. In this study, a novel α-amylase nanobiocatalytic system was constructed based on the allosteric activation of the enzyme and its immobilization on a natural nanostructured mineral montmorillonite. The strategy of allosteric modulation and immobilization, equipped the immobilized α-amylase with higher catalytic activity and greater stability (compared to those of free α-amylase) over a broad range of pH values (4.5-9.0) and temperatures (30-80 °C). Kinetic experiments revealed that although the immobilized α-amylase possessed a considerably lower affinity for its substrate, its catalytic activity was higher than that of free α-amylase, likely owing to allosteric modulation. Thus, this study demonstrates a convenient and environmentally benign immobilization strategy to construct a nanobiocatalytic α-amylase system that exploits the phenomenon of allosteric activation of the enzyme and lays the foundation for further industrial applications.
Keywords: Allosteric effect; Enzyme immobilization; Montmorillonite; Nanocatalyst; α-Amylase.
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