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Chinese Journal of Biotechnology ; (12): 1676-1684, 2016.
Article in Chinese | WPRIM | ID: wpr-243690

ABSTRACT

We studied the effect of calcium ion on particle size and pore structure of cross-linked enzyme aggregates (CLEAs) of glucose oxidase, with activity and stability of the enzyme as evaluation criteria. With calcium ion to prepare CLEA significantly decreased particle sizes of CLEAs whilst the pore structures of CLEAs gradually disappeared with the increase of calcium concentration. When glucose oxidase was precipitated at 0.1 mmol/L Ca²⁺, glucose oxidase in CLEA showed the definitive pore structure. Moreover, glucose oxidase activity in CLEA with Ca²⁺ was 1.69 times higher than that without Ca²⁺. Even at Ca²⁺ as high as 1.0 mmol/L, glucose oxidase activity in CLEA was 42% higher than that of CLEA without Ca²⁺. Furthermore, CLEA prepared with 0.1 mmol/L Ca²⁺ not only exhibited higher substrate conversion and operational stability, but also increased the maximum reaction speed. Therefore, calcium ion improved the performance of glucose oxidase in CLEAs.


Subject(s)
Calcium , Chemistry , Cross-Linking Reagents , Enzyme Stability , Enzymes, Immobilized , Glucose Oxidase , Chemistry , Oxidation-Reduction , Particle Size
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