Applied Microbiology and Biotechnology

, Volume 50, Issue 2, pp 193–198

Production of trehalose synthase from a basidiomycete, Grifola frondosa, in Escherichia coli

  • K. Saito
  • H. Yamazaki
  • Y. Ohnishi
  • S. Fujimoto
  • E. Takahashi
  • S. Horinouchi
SHORT CONTRIBUTION

DOI: 10.1007/s002530051276

Cite this article as:
Saito, K., Yamazaki, H., Ohnishi, Y. et al. Appl Microbiol Biotechnol (1998) 50: 193. doi:10.1007/s002530051276

Abstract

The genomic DNA and cDNA for a gene encoding a novel trehalose synthase (TSase) catalyzing trehalose synthesis from α-d-glucose 1-phosphate and d-glucose were cloned from a basidiomycete, Grifola frondosa. Nucleotide sequencing showed that the 732-amino-acid TSase-encoding region was separated by eight introns. Consistent with the novelty of TSase, there were no homologous proteins registered in the databases. Recombinant TSase with a histidine tag at the NH2-terminal end, produced in Escherichia coli, showed enzyme activity similar to that purified from the original G. frondosa strain. Incubation of α-d-glucose 1-phosphate and d-glucose in the presence of recombinant TSase generated trehalose, in agreement with the enzymatic property of TSase that the equilibrium lay far in the direction of trehalose synthesis.

Copyright information

© Springer-Verlag Berlin Heidelberg 1998

Authors and Affiliations

  • K. Saito
    • 1
  • H. Yamazaki
    • 1
  • Y. Ohnishi
    • 1
  • S. Fujimoto
    • 2
  • E. Takahashi
    • 2
  • S. Horinouchi
    • 1
  1. 1.Department of Biotechnology, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan Tel.: +81-3-3812-2111, ext. 5123 Fax: +81-3-5802-2931JP
  2. 2.Nishiki Research Laboratories, Kureha Chemical Industry Co. Ltd., Nishiki-machi, Iwaki-shi, Fukushima 974-8686, JapanJP