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Novel amphiphilic polyvinylpyrrolidone functionalized silicone particles as carrier for low-cost lipase immobilization
Author(s) -
Shan Zhang,
Qianchun Deng,
Ya Li,
Mingming Zheng,
Chuyun Wan,
Zheng Chang,
Hu Tang,
Fenghong Huang,
Jie Shi
Publication year - 2018
Publication title -
royal society open science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.84
H-Index - 51
ISSN - 2054-5703
DOI - 10.1098/rsos.172368
Subject(s) - lipase , polyvinylpyrrolidone , thermostability , amphiphile , polystyrene , polymer , fourier transform infrared spectroscopy , chemical engineering , materials science , silicone , chemistry , polymer chemistry , organic chemistry , nuclear chemistry , copolymer , enzyme , engineering
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.

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