Short communication
Purification and characterization of an extracellular acid trehalase from Lentinula edodes
2001 年 42 巻 5 号 p. 479-482
詳細
2001 年 42 巻 5 号 p. 479-482
Trehalase from the culture filtrate of Lentinula edodes was purified and characterized. Molecular masses were estimated to be 158 kDa and 79-91 kDa by gel filtration and SDS-PAGE under the reduced condition, respectively. The enzyme was composed of two identical subunits and contained carbohydrate molecules. The optimum temperature and pH were obtained at around 40°C and pH 5.0, respectively. The enzyme was stable up to 40°C and in a range pH of 4-10 at 30°C. It cleaved α-1,1 linkages of trehalose, but not α-1,4, α-1,6 or β-1,4 glycosyl linkages, and was defined as an acid trehalase.
