文献类型：期刊文献

英文题名：Immobilization of glycolate oxidase from Medicago falcata on magnetic nanoparticles for application in biosynthesis of glyoxylic acid

作者：Zhu, Hong[1]; Pan, Jiang[1]; Hu, Bin[1]; Yu, Hui-Lei[1]; Xu, Jian-He[1]

机构：[1] Laboratory of Biocatalysis and Bioprocessing, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, 200237, China

年份：2009

卷号：61

期号：3-4

起止页码：174

外文期刊名：Journal of Molecular Catalysis B: Enzymatic

收录：EI(收录号：20095212568279)

语种：英文

外文关键词：Nanomagnetics - Nanoparticles - Fourier transform infrared spectroscopy - Batch reactors - Enzyme immobilization - Enzyme activity - Synthesis (chemical) - Biochemistry - Plants (botany) - Scanning electron microscopy

摘要：Glycolate oxidase was isolated from Medicago falcata Linn. after a screening from 13 kinds of C3 plant leaves, with higher specific activity than the enzyme from spinach. The M. falcata glycolate oxidase (MFGO) was partially purified and then immobilized onto hydrothermally synthesized magnetic nanoparticles via physical adsorption. The magnetic nanoparticles were characterized with scanning electron microscope (SEM), transmission electron microscopy (TEM) and Fourier transform infrared (FT-IR) spectroscopy. The maximum load of MFGO was 56 mg/g support and the activity recovery was 45%. Immobilization of MFGO onto magnetic nanoparticles enhanced the enzyme stability, and the optimum temperature was significantly increased from 15 °C to 30 °C. The immobilized biocatalyst was successfully used in a batch reactor for repeated oxidization of glycolic acid to synthesize glyoxylic acid, retaining ca. 70% of its initial activity after 4 cycles of reaction at 30 °C for nearly 70 h, and its half-life was calculated to be 117 h. ? 2009 Elsevier B.V. All rights reserved.