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    Activity and Thermal Stability Improvements of Glucose Oxidase upon Adsorption on Core-Shell PMMA-BSA Nanoparticles

    Year: 2009

    Journal: Langmuir, 2009, 25 (23), pp 13456–13460, 20100827

    Authors: He C. †‡, Liu J. *‡, Xie L. †, Zhang Q. ‡, Li C. ‡, Gui D. ‡, Zhang G. *†, Wu C. †§

    Last authors: Chi Wu

    Organizations: † 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 ‡ School of Chemistry and Chemical Engineering, Shenzhen University, Shenzhen, Guangdong 518060, China § Department of Chemistry, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong

    Country: China, Hong Kong

    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 °C for 35 h.