食品科学2012，Vol.33Issue(19)：254-258,5.
巨大芽孢杆菌产胞外核糖核酸酶的分离纯化及部分酶学性质研究
Purifi cation and Partial Characterization of Extracellular Ribonuclease from Bacillus megaterium
摘要
Abstract
After amonanium sulfate precipitation followed by ion-exchange chromatography on CM-Sepharose column and Superdex-200 gel-fi ltration, ribonuclease fromBacillus megaterium was purifi ed to electrophoretic homogeneity. Some of its enzymological properties were then explored. The results showed that the enzyme was 606.67-fold purifi ed with specifi c activity of 54272.27 U/mg and recovery rate of 11.37%. The molecular weight was 33.3 kD. Optimum activity of the enzyme was achieved at 52.5℃ and pH 8.5. The enzyme displayed good stability at 20—40℃ and pH 6.0—7.0. The activity of this enzyme was inhibited by Fe2+, Cu2+, SDS, ascorbic acid and oxalic acid.关键词
巨大芽孢杆菌/核糖核酸酶/分离纯化/性质Key words
Bacillus megaterium/ribonuclease/isolation and purifi cation/characterization分类
生物科学引用本文复制引用
赵芯,成丽丽,邓玉,敬海明,唐云明..巨大芽孢杆菌产胞外核糖核酸酶的分离纯化及部分酶学性质研究[J].食品科学,2012,33(19):254-258,5.基金项目
重庆市科学技术委员会重点攻关项目(CSTC，2011AB1027) （CSTC，2011AB1027）
