Uesaka E, Sato M, Raiju M, Kaji A
J Bacteriol. 1978 Mar;133(3):1073-7. doi: 10.1128/jb.133.3.1073-1077.1978.
An alpha-L-arabinofuranosidase (EC 3.2.1.55) from the culture fluid of Rhodotorula flava IFO 0407 grown on beet arabinan as a carbon source has been highly purified. The purified enzyme has a pH optimum of 2.0. The enzyme is unusually acid stable, retaining 82% of its activity after being maintained for 24 h at pH 1.5 and at 30 degrees C. The apparent Km and Vmax values of the enzyme for phenyl alpha-L-arabinofuranoside were determined to be 9.1 mM and 72.5 mumol per min per mg of protein, respectively.
从以甜菜阿拉伯聚糖作为碳源培养的黄红酵母IFO 0407的培养液中高度纯化得到了一种α-L-阿拉伯呋喃糖苷酶（EC 3.2.1.55）。纯化后的酶最适pH为2.0。该酶具有异常的酸稳定性，在pH 1.5和30℃下保持24小时后仍保留其82%的活性。该酶对α-L-阿拉伯呋喃苯糖苷的表观Km值和Vmax值分别测定为9.1 mM和每毫克蛋白质每分钟72.5 μmol。
