Purification and characterization of xylanase from a thermophilic Streptomyces sp. K37.

Acta microbiologica Polonica Pub Date : 2003-01-01
F A Mansour, A A Shereif, M M Nour el-Dein, M I Abou-Dobara, A S Ball
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Abstract

Extracellular xylanase (EC 3.2.1.8) from Streptomyces sp. K37 was purified 33.53 by ultrafiltration and cation exchange chromatography followed by gel filtration chromatography. The optimum pH and temperature for purified xylanase were found to be pH 6.0 and 60 degrees C. The Km and V(max) values of the purified xylanase were 15.4 mg ml(-1) and 0.67 micromole reducing sugar min(-1) ml(-1). High performance liquid chromatography (HPLC) gel filtration of the purified xylanase eluted xylanase activity as a peak corresponding to the molecular weight of about 24.3 kDa while the molecular weight determined by SDS-PAGE was found to be 26.4 kDa. The purified xylanase of Streptomyces sp. K37 was found to be endoxylanase and non arabinose liberating enzyme and was highly glycosylated (73.97%).

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嗜热链霉菌(Streptomyces sp. K37)木聚糖酶的纯化及特性研究。
采用超滤-阳离子交换层析-凝胶过滤层析的方法纯化了Streptomyces sp. K37细胞外木聚糖酶(EC 3.2.1.8)。纯化木聚糖酶的最适pH和温度分别为pH 6.0和60℃,纯化木聚糖酶的Km和V(max)值分别为15.4 mg ml(-1)和0.67微摩尔还原糖min(-1) ml(-1)。纯化后的木聚糖酶经高效液相色谱(HPLC)凝胶过滤洗脱得到的木聚糖酶活性为峰,对应分子量约为24.3 kDa,而SDS-PAGE测定的分子量为26.4 kDa。纯化的链霉菌K37木聚糖酶为内生木聚糖酶和非阿拉伯糖释放酶,且糖基化程度高(73.97%)。
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