从枯草芽孢杆菌中提取甘露聚糖酶的纯化和性质。
Purification and properties of mannanase from Bacillus subtilis.
机构信息
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出版信息
World J Microbiol Biotechnol. 1994 Sep;10(5):551-5. doi: 10.1007/BF00367665.
PMID:24421132
Abstract
Extracellular mannanase from Bacillus subtilis NM-39, an isolate from Philippine soil, was purified about 240-fold with a yield of 7.3% by ammonium sulphate fractionation, DEAE-Toyopearl chromatography and Sephacryl S-200 gel filtration. Its M r was 38 kDa and it had a pI of 4.8 and optimum activity at pH 5.0 and 55°C. It was stable at pH 4 to 9 and below 55°C. The amino acid composition of the enzyme was in the order Gly>Glx>Ser and Asx>Ala.
摘要
菲律宾土壤中分离得到的枯草芽孢杆菌 NM-39 产生的胞外甘露聚糖酶经硫酸铵分级沉淀、DEAE-Toyopearl 层析和 Sephacryl S-200 凝胶过滤，纯化 240 倍，回收率为 7.3%。其相对分子质量为 38 kDa，等电点为 4.8，最适 pH 为 5.0，最适温度为 55°C。该酶在 pH4 到 9 和低于 55°C 的条件下稳定。酶的氨基酸组成顺序为 Gly>Glx>Ser 和 Asx>Ala。
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