Applied Genetics and Molecular Biotechnology

Applied Microbiology and Biotechnology

, Volume 68, Issue 2, pp 213-219

First online:

Cloning and expression of a trehalose synthase from Pseudomonas stutzeri CJ38 in Escherichia coli for the production of trehalose

  • Jin-Ho LeeAffiliated withR&D Center for Bioproducts, CJ Corporation
  • , Kwang-Ho LeeAffiliated withR&D Center for Bioproducts, CJ Corporation
  • , Chang-Gyeom KimAffiliated withR&D Center for Bioproducts, CJ Corporation
  • , Se-Young LeeAffiliated withMacrogen Incorporated
  • , Geun-Joong KimAffiliated withInstitute of Industrial Biotechnology, Inha University
  • , Young-Hoon ParkAffiliated withR&D Center for Bioproducts, CJ Corporation
  • , Sung-Oh ChungAffiliated withR&D Center for Bioproducts, CJ Corporation Email author 

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A novel strain was isolated, Pseudomonas stutzeri CJ38, that enabled direct transformation of maltose to trehalose. In comparison with others reported to date, CJ38 provided a novel trehalose synthase (TSase) without any byproduct, including glucose. Activity analysis, using either maltose or trehalose as a substrate, showed a reversible reaction. There was also no detectable activity of related enzymes with liquid starch and maltooligosaccharides as substrates. Using a malPQ-negative host and MacConkey medium, the TSase gene was cloned in Escherichia coli from CJ38. The resulting sequence contained an open reading frame consisted of 689 amino acids with a calculated molecular mass of 76 kDa. A search for related sequences in various gene and protein data banks revealed a novel family of enzymes that was predicted putatively as a glycosidase or TSase family, with no biochemical evidence. The recombinant enzyme exhibited a high activity toward the substrate maltose, about 50-fold higher than the parent strain and resulted in a high conversion yield (72%) at a relatively high substrate concentration (20%). These results provided the possibility that the strain was effectively used as a potential biocatalyst for the production of trehalose from maltose in a one-step reaction.