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Efficient Production of o-Tagatose Using a Food-Grade Surface Display System

机译:使用食品级表面展示系统高效生产邻塔格糖

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D-Tagatose, a functional sweetener, is commonly transformed from n-galactose by L-arabinose isomerase (l-AI). In this study, a novel type of biocatalyst, L-AI from Lactobacillus fermentum CGMCC2921 displayed on the spore surface of Bacillus subtilis 168, was developed for producing D-tagatose. The anchored i.-AI, exhibiting the relatively high bioactivity, suggested that the surface display system using CotX as the anchoring protein was successfully constructed. The stability of the anchored L-AI was significantly improved. Specifically, the consolidation of thermal stability representing 87% of relative activity was retained even at 80 °C for 30 min, which remarkably favored the production of D-tagatosc. Under the optimal conditions, the robust spores can convert 75% n-galactose (100 g/L) into D-tagatose after 24 h, and the conversion rate remained at 56% at the third cycle. Therefore, this biocatalysis system, which could express the target enzyme on the food-grade vector, was an alternative method for the value-added production of D-tagatose.
机译:D-塔格糖是一种功能性甜味剂,通常通过L-阿拉伯糖异构酶(1-AI)从正半乳糖转化而来。在这项研究中,开发了一种新型的生物催化剂,来自发酵乳杆菌CGMCC2921的L-AI,显示在枯草芽孢杆菌168的孢子表面,用于生产D-塔格糖。具有较高生物活性的锚定的i.-AI表明,成功构建了使用CotX作为锚定蛋白的表面展示系统。锚定的L-AI的稳定性得到显着改善。具体而言,代表相对活性的87%的热稳定性甚至在80°C下保持30分钟也得以保留,这明显有利于D-tagatosc的生产。在最佳条件下,健壮的孢子可以在24小时后将75%的半乳糖(100 g / L)转化为D-塔格糖,并且在第三个循环中转化率保持在56%。因此,这种可以在食品级载体上表达目标酶的生物催化系统是D-塔格糖增值生产的另一种方法。

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