食品与机械2011，Vol.27Issue(5)：75-77,141,4.DOI:10.3969/j.issn.1003-5788.2011.05.018
欧文氏菌乳糖酶的分离纯化及其酶学性质研究
Purification and enzymatic characterization of a β-galactosidase from Erwinia sp.
摘要
Abstract
The β-galactosidase from Erwinia sp. E5 was isolated and purified. The specific enzymatic activity of the purified enzyme was 554. 92 U/mg protein. The properties of this enzyme were characterized. Results showed this enzyme had a maximum activity at 40 ℃ , and more than 40% of the enzymatic activity was kept at 20 ℃. The optimal pH to this enzyme is 7. 0, and 95% of the enzymatic activity was kept under pH 6. 5. Metal cations Mg2+ and Na+ could activate the enzymatic activity while the cation Ca2+ acted as a weak inhibitor. The lactose hydrolysis experiment showed that this enzyme kept a relatively fast reaction speed when the lactose concentration was below 10%.关键词
欧文氏菌/β-半乳糖苷酶/分离纯化/酶学性质研究Key words
Erxvinia/ β-galactosidase/ isolation and purification/ enzymatic characterization引用本文复制引用
夏雨,成玉梁,赵莹,吕源玲,孙震..欧文氏菌乳糖酶的分离纯化及其酶学性质研究[J].食品与机械,2011,27(5):75-77,141,4.基金项目
江苏省自然科学基金(编号:BK2008103) （编号:BK2008103）
教育部博士点基金(编号:200802951022) （编号:200802951022）
