绿色糖单孢菌木聚糖酶的分离纯化与酶学性质研究  

Studies on Purification and Characteristics of Xylanase from Saccharomonospora viridis

作　　者：王子元[1] 王晓宇[1] 谢响明[1] 

机构地区：[1]北京林业大学生命科学与技术学院,中国北京100083

出　　处：《生命科学研究》2012年第2期132-137,共6页Life Science Research

基　　金：国家自然科学基金资助项目(30870028)

摘　　要：木聚糖酶是一种重要的具有工业应用前景的木聚糖降解酶,在充分利用自然资源、保护生态环境等方面具有十分重要的意义.通过硫酸铵分级沉淀及Sephadex G-100凝胶柱层析方法从一株中度耐热耐碱放线菌—绿色糖单孢菌的胞外酶中纯化得到单一的木聚糖酶,相对分子质量为51 kD,酶纯度提高了13.01倍.纯酶最适反应温度为60℃,最适反应pH值为7.0;75℃以下该酶具有良好的热稳定性,在pH 7～10范围内具有较强的耐受力.金属离子Ca2+、Fe2+、Zn2+对该酶具有明显促进作用,Cu2+、Mn2+、Al3+和SDS具有抑制作用而K+,Na+,Mg2+没有明显的作用.该酶为大分子质量的糖基化蛋白,含糖量为21.96%.Xylanase is a promising xylan-degrading enzyme in industry application. It has great significance in the full use of natural resources and protection of the ecological environment. Through ammonium sulfate precipitation and Sephadex G-100 gel-filtration chromatography, a homogeneous protein is separated and pu- rified from a thermostable and alkali tolerant actinomycete--Saccharomonospora viridis. The relative molec- ular mass of purified xylanase is estimated as 51 kD, and the purification multiple of it is enhanced by 13.01. The purified xylanase exhibited the highest activity at 60 ℃ and pH 7.0. At pH 7-10 and below 75 ℃, the enzyme showed high activity and good stability. It was activated by Ca2＋, Fe2＋ and Zn2＋, while inhibited by Cu2＋, Mn2＋, Al3＋ and SDS. In addition, K＋, Na＋, Mg2＋ have no significant influence on the activity of xylanase. It was a kind of high molecule mass glycoprotein containing 21.69% carbohydrate.

关 键 词：绿色糖单孢菌 耐热 耐碱 木聚糖酶 纯化 酶学性质 

分 类 号：Q936[生物学—微生物学]