Abstract
The high catalytic activity, specificity and stability of immobilized lipase have been attracting great interest. How to reduce the cost of support materials has always been a hot topic in this field. Herein, for the development of low-cost immobilized lipase, we demonstrate an amphiphilic polyvinylpyrrolidone (PVP) grafted on silicone particle (SP) surface materials (SP-PVP) with a rational design based on interfacial activation and solution polymerization. Meanwhile, hydrophilic pristine SP and hydrophobic polystyrene-corded silicone particles (SP-Pst) were also prepared for lipase immobilization. SP-PVP was characterized by X-ray diffraction, scanning electron microscopy, X-ray photoelectron spectroscopy, Fourier transform infrared spectroscopy and thermogravimetry. Our results indicated that the lipase loading amount on the SP-PVP composites was about 215 mg of protein per gram. In the activity assay, the immobilized lipase SP-PVP@CRL exhibited higher catalysis activity and better thermostability and reusability than SP@CRL and SP-Pst@CRL. The immobilized lipase retained more than 54% of its initial activity after 10 times of re-use and approximately trended to a steady rate in the following cycles. By introducing the interesting amphiphilic polymer to this cheap and easily obtained SP surface, the relative performance of the immobilized lipase can be significantly improved, facilitating interactions between the low-cost support materials and lipase.
Highlights
The high effectiveness, high specificity, low cost and environment-friendly properties make biocatalysts the preferable alternative to the classic chemical modifications especially in the pharmaceutical chemistry and food modification with the rapid development of green and sustainable chemistry [1,2]
These results indicated that Pst and PVP had been grafted onto the surface of the silicone particle (SP), and the composite particles Pst-PVP and SP-PVP had been transmittance (%)
The results demonstrated that PVP had been grafted onto the surface of the SP, which was consistent with the IR results
Summary
The high effectiveness, high specificity, low cost and environment-friendly properties make biocatalysts the preferable alternative to the classic chemical modifications especially in the pharmaceutical chemistry and food modification with the rapid development of green and sustainable chemistry [1,2]. Immobilizing lipase on some cheap and obtained supports in different ways can lead to the properties of enhanced performance, improved stability and prolonged reusability, reducing the cost of biocatalysts in enzyme application [8,9,10]. Inorganic supports such as silica [32,33,34], titania (TiO2) [35,36], carbon nanotube [37,38,39], Fe2O3/Fe3O4 [40] and hydrotalcite (LDHs) [41] have been proved to be of great potential for lipase confinement [3] For their large surface areas, low cost, inertness and stability at elevated temperatures, silicone particles (SP) have drawn great focus in enzyme immobilization. The physical properties, relative activity, stability and reusability were all analysed in this work
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