Tavobilov I M, Rodionova N A, Akparov V Kh, Bezborodov A M
Prikl Biokhim Mikrobiol. 1982 Sep-Oct;18(5):671-80.
From the preparation of xylanase of the fungus Aspergillus niger 15 exo-1,4-beta-xylosidase was isolated by means of ethanol fractionation and chromatography on columns of Sephadex G-50, cellulose DE-52, Sephadex SP C-50, Sephadex G-200. The isolated enzyme (with the purification degree as calculated per protein 199, and yield with respect to activity 42.5%) was homogeneous during gel filtration, polyacrylamide gel electrophoresis in the presence and absence of Na dodecyl sulfate, ultracentrifugation and isoelectric focusing. Exo-1,4-beta-xylosidase had a molecular mass of 253,000 as shown by gel filtration and 122,000 as shown by Na dodecyl sulfate polyacrylamide gel electrophoresis; its sedimentation coefficient was 10.6 S and isoelectric point was pI 4.9. The specific activity of the homogeneous enzyme was 35.2 u./mg protein with respect to p-nitrophenyl-beta-D-xylopyranoside and 30.2 u./mg protein with respect to xylobiose.
从黑曲霉15菌株的木聚糖酶制备物中，通过乙醇分级分离以及在Sephadex G - 50、纤维素DE - 52、Sephadex SP C - 50、Sephadex G - 200柱上进行色谱分离，分离得到外切 - 1,4 - β - 木糖苷酶。分离得到的酶（以蛋白质计算的纯化程度为199，相对于活性的产率为42.5%）在凝胶过滤、有无十二烷基硫酸钠存在下的聚丙烯酰胺凝胶电泳、超速离心和等电聚焦过程中均表现为均一。通过凝胶过滤显示外切 - 1,4 - β - 木糖苷酶的分子量为253,000，通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳显示为122,000；其沉降系数为10.6 S，等电点为pI 4.9。该均一酶相对于对硝基苯基 - β - D - 吡喃木糖苷的比活性为35.2 u./mg蛋白质，相对于木二糖的比活性为30.2 u./mg蛋白质。
