Production of trehalose synthase from a basidiomycete, Grifola frondosa, in Escherichia coli |
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| Authors: | K. Saito H. Yamazaki Y. Ohnishi S. Fujimoto E. Takahashi S. Horinouchi |
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| Affiliation: | (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: +81-3-5802-2931, JP;(2) Nishiki Research Laboratories, Kureha Chemical Industry Co. Ltd., Nishiki-machi, Iwaki-shi, Fukushima 974-8686, Japan, JP |
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| 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. Received: 12 January 1998 / Received revision: 20 February 1998 / Accepted: 20 March 1998 |
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