【摘 要】
：
L-Rhamnulose-1-phosphate aldolase from a thermophilic source (Thermotoga maritima MSB8) (RhaDT.mari) was heterologously overexpressed in Escherichia coli with a high expression level and the stereosel
【机 构】
：
Key Laboratory of Carbohydrate Chemistry and Biotechnology,Ministry of Education,School of Biotechno
【出 处】
：
2015中国酶工程与糖生物工程学术研讨会
论文部分内容阅读
L-Rhamnulose-1-phosphate aldolase from a thermophilic source (Thermotoga maritima MSB8) (RhaDT.mari) was heterologously overexpressed in Escherichia coli with a high expression level and the stereoselectivity of this enzyme with or without Nus tag was investigated.To follow green chemistry principles by avoiding the direct use of expensive and unstable DHAP, we employed the one-pot four-enzyme system developed before and synthesized a series of rare sugars (D-psicose, D-sorbose,L-tagatose and L-fructose) starting from relatively inexpensive compounds such as racemic glycerol 3-phosphate.using our one-pot four-enzyme system.To the best of our knowledge, this is the first use of RhaD from a thermophilic source for rare sugar synthesis and the temperature tolerance of this enzyme paves the path for large scale fermentation.
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