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Published on: October 24, 2016
Biochemical identification of a hyperthermostable l-ribulose 3-epimerase from Labedella endophytica and its
Ding Chen1, Jiajun Chen1, Xiaoyong Liu2
1State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; International Joint Laboratory on Food Safety, Jiangnan University, Wuxi, Jiangsu 214122, China.
Abstract:
Currently, low sugar and low energy have become an important trend in the food industries. Therefore, the bioconversion of the functional low-calorie rare sugars attracts more and more attention. l-Ribulose 3-epimerase (LREase) belongs to the ketose 3-epimerase (KEase) family, which could not only efficiently catalyze the reversible C-3 epimerization between l-ribulose and l-xylulose but also between d-fructose and d-allulose. In this paper, a hyperthermostable LREase from Labedella endophytica was identified and characterized. It exhibited maximum catalytic activity at pH 6.0 and 80 °C with 1 mM Ni2+. In the presence of Co2+, the t1/2 values at 60, 65, and 70 °C were 37.7, 9.0, and 4.6 h, respectively, and Tm value was 80.9 °C. From 500 g/L d-fructose, it could produce 154.2 g/L d-allulose with a conversion rate of 30.8% in 10 h. In view of its strong thermostability and high catalytic efficiency, L. endophytica LREase might be a good potential alternative for d-allulose industrial production.
