生物加工过程2016，Vol.14Issue(5)：51-55,5.DOI:10.3969/j.issn.1672-3678.2016.05.010
Bacillus sublitis JH 1木聚糖酶的纯化及酶学性质
Purification and characterization of xylanase from Bacillus sublitis JH-1
摘要
Abstract
We purified and characterized xylanase from Bacillus sublitis JH-1. The crude enzyme was purified by ammonium sulfate fractionation,dialysis desalination and DEAE-Sepharose FF anion exchange chromatography.The specific activity was 75 899. 68 U/mg,and its subunit molecular weight was 3. 45× 104 determined by SDS-PAGE.The xylanase showed optimal activity at pH 6. 0.It retained more than 75%of its maximum activity at pH 6. 0 for 2 h,and the higher the pH,the faster the activity lost. The optimal temperature was 55℃ and it retained more than 70% of its maximum activity between 50 and 60℃ for 2 h. Metal ions Fe2 +, Mg2+, Ca2+, Zn2+, Ba2+ and low concentration ( 5 mmol/L) of Fe3+have obviously promoting effect on xylanase activity,whereas Mn2+ and high concentration(10 mmol/L) of Fe3+inhibited the enzyme.关键词
枯草芽孢杆菌/木聚糖酶/纯化/弱阴离子交换层析/酶学性质Key words
Bacillus sublitis/xylanase/purification/anion exchange chromatography/enzymatic properties分类
生物科学引用本文复制引用
邵婷婷,王春明,李蘅香,钟超,雍晓雨,贾红华,周华,韦萍..Bacillus sublitis JH 1木聚糖酶的纯化及酶学性质[J].生物加工过程,2016,14(5):51-55,5.基金项目
国家重点基础研究发展计划（973计划）（2013CB733500）；国家科技支撑计划 （）
