Novel amphiphilic polyvinylpyrrolidone functionalized silicone particles as carrier for low-cost lipase immobilization. Issue 6 (13th June 2018)

• Record Type: Journal Article
• Authors: Zhang, Shan; Deng, Qianchun; Li, Ya; Zheng, Mingming; Wan, Chuyun; Zheng, Chang; Tang, Hu; Huang, Fenghong; Shi, Jie
• Is Part Of: Royal Society open science. Volume 5:Issue 6(2018)
• Publication Date: 2018-06-13
• Subjects: amphiphilic, polyvinylpyrrolidone -- silicone, immobilization; Science -- Periodicals; 500
• DOI: 10.1098/rsos.172368
• Languages: English
• ISSNs: 2054-5703

Abstract

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.