Purification and properties of a xylanase from Streptomyces lividans.
Purification and properties of a xylanase from Streptomyces lividans.
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浅青紫链霉菌木聚糖酶的纯化和特性。
DOI：
10.1042/bj2390587
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发表时间：
1986
期刊：
影响因子：
--
通讯作者：
D. Kluepfel
中科院分区：
文献类型：
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作者：
R. Morosoli;J. Bertrand;F. Mondou;F. Shareck;D. Kluepfel
对变铅青链霉菌1326纤维素酶阴性突变株产生的胞外木聚糖酶进行了纯化。纯化的酶的表观相对分子质量为43,000，等电点为5.2。该酶的最适pH和最适温度分别为6.0℃和60℃，最适Km和Vmax。用燕麦可溶性木聚糖测定值为每毫克酶0.78毫克/毫升和0.85摩尔/分钟。该木聚糖酶对CM-纤维素和对-硝基苯基-β-D-木糖苷无活性。该酶降解木聚糖，主要产生木二糖，低聚木糖和少量木糖的混合物作为最终产品。它对β-1，4-D-木聚糖的作用模式表明它是一种β-1，4-内切木聚糖酶(EC 3.2.1.8)。
An extracellular xylanase produced by a cellulase-negative mutant strain of Streptomyces lividans 1326 was purified to homogeneity. The purified enzyme has an apparent Mr of 43,000 and pI of 5.2. The pH and temperature optima for the activity were 6.0 and 60 degrees C respectively, and the Km and Vmax. values, determined with a soluble oat spelts xylan, were 0.78 mg/ml and 0.85 mmol/min per mg of enzyme. The xylanase showed no activity towards CM-cellulose and p-nitrophenyl beta-D-xyloside. The enzyme degraded xylan, producing mainly xylobiose, a mixture of xylo-oligosaccharides and a small amount of xylose as end products. Its pattern of action on beta-1,4-D-xylan indicates that it is a beta-1,4-endoxylanase (EC 3.2.1.8).