원문정보
초록
영어
Trehalose is a natural alpha-linked disaccharide formed by an α, α-1, 1-glucoside bond between two α-glucose units. Emerging areas of applications of trehalose are in pharmaceuticals as stabilizer of vaccines during storage, in cosmetics as a liposome stabilizer and in food industry as stable sweetener.
Currently, trehalose has been produced from food-grade starch or maltodextrins by the enzymatic
process [1]. However, low solubility of substrates and high viscosity of reaction mixture made this
process less attractive. As an alternative approach, the use of metabolic engineering can improve the production of trehalose in the culture of microorganisms. The enhanced production of trehalose was previously demonstrated by the heterologous expression of E.coli genes in Corynebacterium
glutamicum [2].
We aimed to enhance the production of trehalose by metabolic engineering of E.coli. In this
presentation, we explored the trehalose production in. E.coli by overexpressing endogeneous trehalose biosynthetic operon (otsBA) encoding Trehalose-6-phosphate phosphatase and trehalose-6-phosphate synthase. These genes were amplified by PCR, sequenced and cloned into pTrc99A vector. This recombinant DNA was introduced into E.coli cells. The effects of different E.coli strains, culture medium and temperature, expression vector, IPTG induction, and salt concentration on trehalose production were investigated.