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Published on: June 20, 2019
Ultrahigh Enzyme Activity Assembled in Layered Double Hydroxides via Mg(2+)-Allosteric Effector
Min Wang1, Shu-Wan Huang1, Dan Xu1
1State Key Laboratory of Analytical Chemistry for Life Science and Collaborative Innovation Center of Chemistry for Life Sciences, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing 210093, China.
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.
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