Synthesis and Effect of Modification On Methacylate - Acrylate Microspheres for Trametes Versicolor Laccase Enzyme Immobilization

被引:4
|
作者
Mazlan, Siti Zulaikha [1 ]
Abu Hanifah, Sharina [1 ]
机构
[1] Univ Kebangsaan Malaysia, Fac Sci & Technol, Sch Chem Sci & Food Technol, Ukm Bangi 43600, Selangor, Malaysia
来源
2014 UKM FST POSTGRADUATE COLLOQUIUM: PROCEEDINGS OF THE UNIVERSITI KEBANGSAAN MALAYSIA, FACULTY OF SCIENCE AND TECHNOLOGY 2014 POSTGRADUATE COLLOQUIUM | 2014年 / 1614卷
关键词
Laccase; synthetic; Methacrylate; Microsize; Covalent binding; BIOSENSOR; PEROXIDASE; REMOVAL; BEADS;
D O I
10.1063/1.4895206
中图分类号
O59 [应用物理学];
学科分类号
摘要
Immobilization of laccase on the modified copolymer methacrylate-acrylate microspheres was studied. A poly (glycidyl methacrylate-co-n-butyl acrylate) microsphere consists of epoxy groups were synthesized using suspension photocuring technique. The epoxy group in poly (GMA-nBA) microspheres were converted into amino groups with aldehyde group. Laccase immobilization is based on having the amino groups on the enzyme surface and aldehyde group on the microspheres via covalent binding. Fourier transform infrared spectroscopy (FT-IR) analysis proved the successful surface modification on microspheres. The FTIR spectrum shows the characteristic peaks at 1646 cm-1 assigned to the conformation of the polymerization that took place between monomer GMA and nBA respectively. In addition, after modification, FTIR peaks that assigned to the epoxy ring (844 cm-1 and 904 cm-1) were decreased. The results obtained from FTIR method signify good agreement with the epoxy content method. Hence, the activity of the laccase-immobilized microspheres increased upon increasing the epoxy content. Furthermore, poly (GMA-nBA) exhibited uniform microspheres with below 2 mu m surface. Immobilized enzyme showed a broader pH profile and higher temperature compared native enzyme.
引用
收藏
页码:263 / 268
页数:6
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