摘要
利用硫酸铵盐析缓冲液透析、聚乙二醇浓缩、DEAE-Sepharose FF窝子交换层析等方法，纯化了枯草芽孢杆菌WD-23β-甘露聚糖酶，并研究了其酶学性质。结果表明：纯化的枯草芽孢杆菌WD-23β-甘露聚糖酶的分子质量约为40 ku，酶的纯化倍数为14.1倍；最适反应pH和pH稳定范围分别为5．6和5．0～7．0；最适反应温度和温度稳定范围分别为55℃和40～70℃；Ca2＋对该酶的促进作用最为明显，Li＋的抑制作用最明显。
The objective of this study was to purifyβ-mannase from Bacillus subtilis WD-23 and examine its enzymology properties. This study used the combining methods of ammonium sulfate, semi-permeable membrane dialysis, polyethy-lene glycol concentration, DEAE-Sepharose FF ion exchange chromatography, Sephadex G-75 gel filtration and SDS-PAGE gel electrophoresis to purifyβ-mannase. The result showed that the purified ratio ofβ-mannase of B. subtilis WD-23 was 14.1 by using the above methods, and the molecular mass was about 40 ku, the optimal pH and the stability range of pH were 5.6 and 5.0-7.0 respectively, and optimal temperature and the stability range of temperature were 55℃ and 40-70℃ separately, Ca2 ＋ was the most obvious effect on the activation of the enzyme, on the contrary, the in-hibitory effect of Li＋ was the most obvious.
出处
《南京林业大学学报（自然科学版）》
CAS
CSCD
北大核心
2014年第3期88-92,共5页
Journal of Nanjing Forestry University：Natural Sciences Edition
基金
哈尔滨市科技局攻关项目(2008AA6B6BN025
GJ2011GG002112)
