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Updated: Mar 19, 2026

Rapid One-step Enzymatic Synthesis and All-aqueous Purification of Trehalose Analogues
Published on: February 17, 2017
Reaction Mechanism of a New Glycosyltrehalose-hydrolyzing Enzyme Isolated from the Hyperthermophilic Archaeum,
1a Applied Bioresearch Center , Kirin Brewery Co., Ltd ., 3 Miyaharaeho, Takasakishi, Gunma 370-12 , Japan.
Abstract:
Amylolytic activity, which converts soluble starch to α,α-trehalose (trehalose), was found in the cell homogenate of the hyperthermophilic acidophilic archaeum, Sulfolobus solfataricus KM1. Two enzymes, a glycosyltransferase and an α-amylase, which were essential for this activity were identified. The α-amylase was purified to homogeneity on SDS-PAGE. The α-amylase catalyzed the hydrolysis of glycosyltrehaloses to trehalose. Analysis of the reaction products, kinetic parameters, and experimental findings using (3)H-labeIed substrates indicated that the α-amylase hydrolyzed only the α-1,4 glucosidic linkage adjacent to the trehalose unit of the glycosyltrehaloses. Six strains of the Sulfolobaceae family examined were observed to have the glycosyltrehalose-hydrolyzing enzyme, the α-amylase.
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