碩士 / 大葉大學 / 生物產業科技學系 / 100 / Trehalose is a new multi-functional disaccharide, it exists in many nature body, not only as a resrve energy and carbon source, but also help resist harsh environment, and has the ability to stabilize biological marcomolecules, trehalose is widely applied in the food, cosmetics and pharmaceutical industries. Trehalose synthase is one of the pathways employed organism to synthesize trehalose. It catalyzes the reversible conversion of maltose into trehalose by intramolecular transglucosylation. This study using a new recombinant Picrophilus torridus trehalose synthase(PTTS) mutant R523P, analyze the biochemical properties.
Thermal stability for enzyme purification, enzyme kinetics, temperature (20℃-65℃) and pH(3-8) values for trehalose conversion rate. Experimental results show that this enzyme (R523P) at 40℃, the reaction of 4 hours, pH6, its conversion rate of trehalose in PTTS-wild type to 50.58±0.67%, and by product of glucose reduction in the 7.92±0.06%. Stability in thetemperature, 70℃ still maintain the 94.31±0.0135% of relative activity. The pH stability, when the pH reached 8, the relative activity of 62.49±0.61% also maintain and expand the reaction range of pH. In this study, pointed out that the mutant enzyme (R523P) reduce glucose produced and expand the scope of the reaction conditions. This suggests in its future industry and raise the production of trehalose would be of great potential.
| Identifer | oai:union.ndltd.org:TW/100DYU00111006 |
| Date | January 2012 |
| Creators | Lin, Che-Hung, 林哲弘 |
| Contributors | Chang, Shu-Wei, 張淑微 |
| Source Sets | National Digital Library of Theses and Dissertations in Taiwan |
| Language | zh-TW |
| Detected Language | English |
| Type | 學位論文 ; thesis |
| Format | 59 |
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