Assembly of graphene oxide-enzyme conjugates through hydrophobic interaction.
Assembly of graphene oxide-enzyme conjugates through hydrophobic interaction.
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DOI：
10.1002/smll.201101695
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发表时间：
2012-01
期刊：
影响因子：
13.3
通讯作者：
Yan Zhang;Jingyan Zhang;Xuelei Huang;Xuejiao Zhou;Haixia Wu;Shouwu Guo
中科院分区：
文献类型：
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作者：
Yan Zhang;Jingyan Zhang;Xuelei Huang;Xuejiao Zhou;Haixia Wu;Shouwu Guo
氧化石墨烯(GO)的生物化学和生物医学应用主要依赖于生物分子与其之间的相互作用。此前有报道称，由于酶与GO之间的静电相互作用，GO-酶结合物的生物活性降低。本文报道了在化学还原氧化石墨烯(CRGO)上固定辣根过氧化物酶(HRP)和草酸氧化酶(OXX)的方法。这些酶可以直接吸附在CRGO上，酶载量是GO的10倍，最大酶载量分别达到1.3 mg mg(-1)和12 mg mg(-1)。值得注意的是，CRGO减少的越多，酶的负载量就越高。与GO-HRP相比，CRGO-HRP具有更高的酶活性和稳定性。CRGO-酶结合物的优异性能归功于酶和CRGO之间的疏水相互作用。CRGO-酶偶联物的疏水相互作用模式可以应用于其他疏水蛋白，从而显著提高固定化蛋白的性能。结果表明，CRGO是一种潜在的高效固定化酶的底物，是一种理想的高分子载体和生物传感器。
Biochemical and biomedical applications of graphene oxide (GO) critically rely on the interaction of biomolecules with it. It has been previously reported that the biological activity of the GO-enzyme conjugate decreases due to electrostatic interaction between the enzymes and GO. Herein, the immobilization of horseradish peroxidase (HRP) and oxalate oxidase (OxOx) on chemically reduced graphene oxide (CRGO) are reported. The enzymes can be adsorbed onto CRGO directly with a tenfold higher enzyme loading than that on GO, and maximum enzyme loadings reach 1.3 and 12 mg mg(-1) for HRP and OxOx, respectively. Significantly, the more CRGO is reduced, the higher the enzyme loading. The CRGO-HRP conjugates also exhibit higher enzyme activity and stability than GO-HRP. Excellent properties of the CRGO-enzyme conjugates are attributed to hydrophobic interaction between the enzymes and the CRGO. The hydrophobic interaction mode of the CRGO-enzyme conjugates can be applied to other hydrophobic proteins, and thus could dramatically improve the performance of immobilized proteins. The results indicate that CRGO is a potential substrate for efficient enzyme immobilization, and is an ideal candidate as a macromolecule carrier and biosensor.