Ultrahigh Enzyme Activity Assembled in Layered Double Hydroxides via Mg²⁺-Allosteric Effector

Abstract

It is well-known that some metal ions could be allosteric effectors of allosteric enzymes to activate/inhibit the catalytic activities of enzymes. In nanobiocatalytic systems constructed based on the positive metal ion-induced allosteric effect, the incorporated enzymes will be activated and thus exhibit excellent catalytic performance. Herein, we present an environmentally friendly strategy to construct a novel allosteric effect-based β-galactosidase/Mg-Al layered double hydroxide (β-gal/Mg-Al-LDH) nanobiocatalytic system via the delamination-reconstruction method. The intercalated β-gal in the LDH galleries changes its conformation significantly due to the Mg(2+)-induced allosteric interactions and other weak interactions, which causes the activation of enzymatic activity. The β-gal/Mg-Al-LDH nanobiocatalytic system shows much higher catalytic activity and affinity toward its substrate and about 30 times higher catalytic reaction velocity than the free β-gal, which suggests that Mg(2+)-induced allosteric effect plays a vital role in the improvement of enzymatic performance.