D-阿洛糖-3-表異構酶在稀有糖生產中的固定化方法與應用
學生姓名:
賴昱亘
指導教授:
方翠筠
學期:
114下
摘 要:
D-Allulose 3-epimerase (DAEase), also known as D-psicose 3-epimerase (DPEase), plays a crucial role in the biosynthesis of the low-calorie rare sugar D-allulose. Improving enzyme expression efficiency and enhancing catalytic performance are essential steps toward achieving cost-effective and large-scale production. In the first study, the DAEase gene derived from Agrobacterium tumefaciens was heterologously expressed in Escherichia coli. Reaction parameters, including pH, temperature, and metal ion supplementation, were systematically optimized to maximize catalytic performance. Under optimized conditions, efficient conversion of fructose to D-allulose was achieved, demonstrating the scalability of enzymatic production and providing a practical framework for industrial application. To further enhance operational stability and reusability, the second study developed immobilization strategies for Clostridium cellulolyticum DAEase (CcDAE). Compared with the free enzyme, the immobilized forms exhibited improved thermal stability, broader pH tolerance, and enhanced storage stability. Notably, the directionally immobilized system demonstrated higher catalytic efficiency. In addition, the immobilized biocatalysts showed good reusability and maintained high conversion. Overall, these findings highlight the potential of DAEase as an efficient and industrially promising biocatalyst for D-allulose production, supporting its application in functional foods and sustainable rare sugar biomanufacturing.
專題討論摘要_11432047_賴昱亘.pdf