A Trehalase from a Green Alga, Lobosphaera sp. and Condensation Catalyzed by the Enzyme

概要

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A unicellular green alga identified as Lobosphaera sp. was selected as a sourse of trehalase. The alga grew well heterotrophically to produce intracellular trehalase. The enzyme was highly purified and characterized. The molecular mass of the native enzyme and that of subunit were estimated to be 400 kDa and 180-200 kDa, respectively. The enzyme was most active at pH 5.5 and at 65t and stable between pH 4-9 and below 65°C. The enzyme specifically hydrolyzed α, α'-trehalose to produce α- and β-anomers of n-glucose in an almost equal ratio . The enzyme catalyzed the condensation not only of n-glucose but also of 2-deoxy-D-glucose, yielding α, α'-trehalose and 2, 2'-dideoxy-α, α'-trehalose, respectively. Simultaneous incubation of the two monosaccharides resulted in the formation of 2- deoxy-α, α'-trehalose. The enzyme synthesized dideoxy-trehalose (yield, 16%) more than trehalose (5%). Monodeoxy-trehalose was produced most effectively in the reaction of D-glucose and 2-deoxyn- glucose in a weight ratio of 2 : 5 to give a yield of 6%.
日本応用糖質科学会の論文