Production of Trehalose by New Trehalose-producing Enzymes from the Archae

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Amylolytic activity that converts soluble starch to α, α-trehalose, was found in the cell homogenate of the hyperthermophilic archae, Sulfolobus. Purification of the activity using new reliable assay methods showed two enzymes to be essential for the activity. The reaction mechanisms of the enzymes were examined by analysis of the reaction products with the two enzymes on maltooligosaccharides using <SUP>1</SUP>H. and <SUP>13</SUP>C-NMR spectra and HPLC. One of the enzymes was a new glycosyltransferase which catalyzed the conversion of maltooligosaccharides to the corresponding glycosyltrehaloses with atrehalose structure as an end unit. The other was a new a-amylase which hydrolyzed the glycosyltrehaloses to isolate trehalose specifically. The genes encoding the enzymes were cloned and expressedin E. coli. The yield of trehalose from starch amounted to 80% using the two enzymes and debranching enzyme.
日本応用糖質科学会の論文