A new metal-chelated beads for reversible use in uricase adsorption
A new metal-chelated beads for reversible use in uricase adsorption
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DOI：
10.1016/j.molcatb.2007.10.005
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发表时间：
2008-03-03
影响因子：
--
通讯作者：
Denizli, Adil
中科院分区：
文献类型：
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作者：
Akgol, Sinan;Oztuerk, Nevra;Denizli, Adil
通过乙二醇二甲基丙烯酸酯（EGDMA）与n-乙烯基咪唑（Vim）的共聚，制备了平均粒径为150-200 μ m的聚（乙二醇二甲基丙烯酸酯-n-乙烯基咪唑）[poly（EGDMA-VIM）]珠粒。聚（EGDMA-VIM）珠的平均孔径为550 nm。通过元素分析表征共聚物珠粒组合物，发现每个Vim单体单元含有五个EGDMA单体单元。聚（EGDMA-VIM）珠具有59.8m2/g的比表面积。聚-（EGDMA-VIM）珠，其特征在于通过溶胀研究和SEM。将Cu ~（2+）离子螯合在聚乙二醇二甲基甲酰胺-乙烯基吡咯烷酮（poly（EGDMA-VIM））微球上，并将其用于猪肝中尿酸酶的吸附。聚（EGDMA-VIM）-Cu 2+珠的最大尿酸酶吸附容量为118.3 mg/g，在pH 6.0。固定化尿酸酶（poly（EGDMA-VIM）-Cu 2+）的Km值（91.95 × 10（-3）mM）高于游离酶的Km值（7.5 × 10（-3）mM）。对于游离酶，V-max计算为0.012 μ mol/min mg蛋白质。对于固定化酶，V-max计算为1.44 μ mol/min mg蛋白质。游离酶在35天内失去全部活性。固定化酶在相同时间内保持了80%的酶活力。发现储存稳定性随着固定化而增加。结果表明，该酶可反复吸附和解吸，吸附量和酶活性无明显损失。(c)2007 Elsevier B. V.保留所有权利。
Poly(ethylene glycol dimethacrylate-n-vinyl imidazole) [poly(EGDMA-VIM)] beads (average diameter 150-200 mu m) was prepared by copolymerizing ethylene glycol dimethacrylate (EGDMA) with it-vinyl imidazole (VIM). Average pore size of poly(EGDMA-VIM) beads was 550 nm. The copolymer beads composition was characterized by elemental analysis and found to contain five EGDMA monomer units each VIM monomer unit. Poly(EGDMA-VIM) beads had a specific surface area of 59.8 m(2)/g. Poly-(EGDMA-VIM) beads were characterized by swelling studies and SEM. Cu2+, ions were chelated on the poly(EGDMA-VIM) beads, then these beads were used in the adsorption of uricase from Porcine Liver in batch system. The maximum uricase adsorption capacity of the poly(EGDMA-VIM)-Cu2+ beads was observed as 118.3 mg/g at pH 6.0. The K-m values for immobilized uricase (poly(EGDMA-VIM)-Cu2+) (91.95 x 10(-3) mM) was higher than that of free enzyme (7.5 x 10(-3) mM). V-max was calculated as 0.012 mu mol/min mg protein for the free enzyme. For the immobilized enzyme, V-max was calculated as 1.44 mu mol/min mg protein. Free enzyme lose all of original activity in 35 days. On the other hand immobilized enzyme preserved 80% of original activity in same time. Storage stability was found to increase with immobilization. It was observed that enzyme could be repeatedly adsorbed and desorbed without significant loss in adsorption capacity or enzyme activity. (c) 2007 Elsevier B.V. All rights reserved.