Article ID Journal Published Year Pages File Type
1358736 Bioorganic & Medicinal Chemistry Letters 2015 4 Pages PDF
Abstract

l-Rhamnulose-1-phosphate aldolase from a thermophilic source (Thermotoga maritima MSB8) (RhaDT.mari) was heterologously overexpressed in Escherichia coli and the stereoselectivity of this enzyme with or without Nus tag was investigated. We also applied this enzyme to the synthesis of rare sugars d-psicose, d-sorbose, l-tagatose and l-fructose 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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Physical Sciences and Engineering Chemistry Organic Chemistry
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