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Difference in enzyme activity and conformation of glucose oxidase before and after purification |
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| Authors: | Guoliang Dai Jinru Li Long Jiang |
| Institution: | a National Microgravity Lab, Institute of Mechanics, Chinese Academy of Sciences, Beijing 100080, People's Republic of China b Center of Molecular Sciences, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100101, People's Republic of China |
| Abstract: | Enzyme activity of commercial glucose oxidase was enhanced after purification through a strong anionic exchange resin. In order to get a better insight into this phenomenon, surface pressure–area (π–A) isotherms and surface pressure–time (π–t) isotherms was used to study the interaction and the absorption at different pH values of the subphases between octadecylamine and glucose oxidase purified by a styrene system quaternary ammonium type strongly basic anionic exchange resin. Circular dichroism (CD), electrophoresis and enzyme activity measurements were conducted to study these phenomena. A preliminary hypothesis has been suggested to explain why the enzyme activity of purified glucose oxidase was higher than that of the commercial one. |
| Keywords: | GOD Purification Surface pressure–area isotherms Surface pressure–time isotherms Octadecylamine |
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