嗜热真菌金耳囊菌（Thermoascus aurantiacus）中α-D-葡萄糖醛酸酶的纯化与特性分析
Purification and characterization of an alpha-D-glucuronidase from a thermophilic fungus, Thermoascus aurantiacus.
作者信息
Khandke K M, Vithayathil P J, Murthy S K
机构信息
Department of Biochemistry, Indian Institute of Science, Bangalore.
出版信息
Arch Biochem Biophys. 1989 Nov 1;274(2):511-7. doi: 10.1016/0003-9861(89)90464-5.
An alpha-D-glucuronidase was purified from the culture filtrates of Thermoascus aurantiacus. A simple colorimetric method for its assay is reported. The enzyme is a single polypeptide chain with a molecular weight of 118,000. It acts optimally at pH 4.5. It shows maximum activity at 65 degrees C. The t 1/2 at 70 degrees C was 40 min. It specifically cleaved the alpha-(1----2) linkage between 4-O-methyl-alpha-D-glucuronic acid and the xylose residue in xylan and several glucurono-xylooligosaccharides.
从橙色嗜热子囊菌的培养滤液中纯化出一种α-D-葡萄糖醛酸酶。报道了一种用于其测定的简单比色法。该酶是一条单多肽链，分子量为118,000。它在pH 4.5时活性最佳。在65℃时表现出最大活性。70℃时的半衰期为40分钟。它能特异性切割木聚糖和几种葡糖醛酸木寡糖中4-O-甲基-α-D-葡萄糖醛酸与木糖残基之间的α-(1→2)键。
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