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.
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Received: 12 January 1998 / Received revision: 20 February 1998 / Accepted: 20 March 1998
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Saito, K., Yamazaki, H., Ohnishi, Y. et al. Production of trehalose synthase from a basidiomycete, Grifola frondosa, in Escherichia coli . Appl Microbiol Biotechnol 50, 193–198 (1998). https://doi.org/10.1007/s002530051276
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DOI: https://doi.org/10.1007/s002530051276