碩士 / 國立中興大學 / 化學工程學系所 / 104 / The employment of immobilized trehalose synthase for the production of trehalose from maltose generally lead to the generation of reaction byproduct, glucose, which needs to be removed. This separation of glucose from trehalose can be facilitated by the converting glucose into gluconic acid with glucose oxidase. In this study, the effect of hydrogen peroxide scavenger, MnO2, on the operation stability of Immobead 150-immobilized glucose oxidase was study. Diatomite-supported manganese dioxide was prepared and characterized. The diatomite with manganese dioxide loading capacity of 100.36 mg/g silica exhibited the optimal catalytic ability, leading to the highest enzyme specific activity of 645.14 U/mg protein and the lowest residual hydrogen peroxide concentration of 15.2 mM. The specific activity of glucose oxidase and the concentration of hydrogen peroxide were 269.00 U/mg protein and 39.8 mM, respectively, after being incubated in phosphate buffer containing glucose for 1 day. In repeated-batch operations, the activity of immobilized enzyme declined after 4 cycles and 8 cycles at pH 7.0 and pH 8.0, respectively, because of the increase in H2O2 concentration possibly resulting from the reduction in scavenging capability of the diamomite-supported MnO2. The results of ICP-MS analysis indicate that the loss in scavenging activity can be attributed to the loss of manganese into the reaction medium. Based on the aboved results, the diatomite-supported manganese dioxide was used for glucose oxidase oxidation, is promising for improving the operational stability.
| Identifer | oai:union.ndltd.org:TW/104NCHU5063078 |
| Date | January 2016 |
| Creators | Yi-Sheng Lin, 林宜聖 |
| Contributors | Sung-Chyr Lin, 林松池 |
| Source Sets | National Digital Library of Theses and Dissertations in Taiwan |
| Language | zh-TW |
| Detected Language | English |
| Type | 學位論文 ; thesis |
| Format | 64 |
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