The Hefei National Laboratory for Physical Sciences at Microscale and Department of Chemical Physics, University of Science and Technology of China, Hefei, Anhui 230026, China.
Langmuir. 2009 Dec 1;25(23):13456-60. doi: 10.1021/la9019124.
The interaction and adsorption of enzyme, glucose oxidase (GOx), on poly(methyl methacrylate)-bovine serum albumin (PMMA-BSA) particles were studied by using a quartz crystal microbalance with dissipation (QCM-D) and laser light scattering (LLS). The enzyme was irreversibly immobilized on the PMMA-BSA particle surface. The amount of enzyme immobilized on PMMA-BSA particles and the enzymatic activity were determined by UV/vis measurements. The influences of pH and ionic strength on the adsorption indicate that the electrostatic interaction plays a major role on the immobilization. The adsorbed GOx can retain at least 80% of the free enzyme activity. Thermal stability studies reveal that the adsorbed GOx only losses 28% of its activity in comparison with a 64% activity loss of free GOx when it is incubated at 50 degrees C for 35 h.
通过石英晶体微天平耗散（QCM-D）和激光光散射（LLS）研究了酶葡萄糖氧化酶（GOx）与聚甲基丙烯酸甲酯-牛血清白蛋白（PMMA-BSA）颗粒的相互作用和吸附。酶不可逆地固定在 PMMA-BSA 颗粒表面。通过紫外/可见测量确定固定在 PMMA-BSA 颗粒上的酶量和酶活性。pH 和离子强度对吸附的影响表明静电相互作用在固定化中起主要作用。吸附的 GOx 可以保留至少 80%的游离酶活性。热稳定性研究表明，与游离 GOx 的 64%活性损失相比，吸附的 GOx 在 50°C 下孵育 35 小时后仅损失 28%的活性。
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