The Assembly Of Delaminated Layerd Double Hydroxides With Porcine Pancreas Lipase

Layered double hydroxides (LDHs) are of special interest in the development of an efficient biomaterial due to the flexibility in composition as well as a wide variety of properties. The delaminated LDHs have been focused due to the wide opened nanostructure and available interfacial properties. It is believed that the delaminated LDHs are useful for biotechnological applications.In this work, we investigate the assembly of exfoliated LDHs lamellas with porcine pancreas lipase (PPL) in the aqueous suspension.The exfoliated LDHs were initially prepared by the method delaminating lactate-containing LDH in aqueous media. XRD, FE-SEM, AFM, and FTIR, are employed to systematically analyze the resulting composite in detail. For valuation of the composite structure effect on the activities, the bioinorganic materials fabricated by different LDH/PPL mass ratio are investigated respectively, which is also helpful to learn the general assembly mechanism and the biomolecule-inorganic coadjustment in structure. We show that LDH-PPL exhibits enhanced enzymatic activity. The activity efficiency can reach 420%. The protein structure and activity are altered during the assembly. In addition, this work described the assembly models by the interfacial adsorption model of protein.The assembly disciplinarians of PPL and Dela-LDH accord with the Pseudo-second order kinetics model. The assembly can take place fast and firmly without diffuse effect. And the equilibrium isotherm of the assembly can be simulated well with Langmuir model.