Activity and thermal stability improvements of glucose oxidase upon adsorption on core-shell PMMA-BSA nanoparticles.
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.
He
Chuanxin
C
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.
Liu
Jianhong
J
Xie
Laiyong
L
Zhang
Qianling
Q
Li
Cuihua
C
Gui
Dayong
D
Zhang
Guangzhao
G
Wu
Chi
C
D000327:Adsorption; D015374:Biosensing Techniques; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000378:metabolism*; D005949:Glucose Oxidase / Q000737:chemistry* / Q000378:metabolism*; D053758:Nanoparticles / Q000737:chemistry*; D019904:Polymethyl Methacrylate / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000737:chemistry*
D004800:Enzymes, Immobilized; D012710:Serum Albumin, Bovine; D019904:Polymethyl Methacrylate; D005949:Glucose Oxidase