Nanobiocatalyst consisting of immobilized α-amylase on montmorillonite exhibiting enhanced enzymatic performance based on the allosteric effect.

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.
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