约氏不动杆菌LP28低温碱性脂肪酶分离纯化及洗涤性能分析

Purification and characterization of a lipase from Acinetobacter johnsonii LP28 and detergent performance optimization

对菌株LP28发酵产的低温碱性脂肪酶进行了分离纯化,菌体发酵液经过离心、硫酸铵沉淀、DEAE-Sepharose Fast Flow离子交换及Sephadex G-75凝胶过滤等步骤处理,比活力达76.66 U/mg,纯化倍数达36.16倍,回收率为14%。菌株LP28所产的脂肪酶洗涤性能分析显示,洗涤温度在30℃、p H 8.0、加酶量为100 U、洗涤剂添加量为0.25%时,其洗涤效果最佳,去油率达35%。且该酶对多种底物具有特异性,并对蛋白酶及市售洗衣粉也具有一定的稳定性。说明Acinetobacter johnsonii LP28脂肪酶具有洗涤剂添加剂应用前景。

A low temperature alkaline lipase from Acinetobacter johnsonii LP28 was isolated and purified using ammonium sulfate precipitation,Fast Flow DEAE-Sepharose ion exchange and G-75 Sephadex gel filtration. The specific activity was 76. 66 U / mg,and this purification protocol resulted in a 36. 16 fold purification of lipase with 14% final yield. A study on the washing performance of the lipase shows that its optimum temperature was 30 ℃ and p H was 8. 0. The optimal enzyme dosage and detergent dosage were 100 U and 0. 25% respectively. Under the optimum conditions,the detergency was 35%. Results shows that the lipase is specific to a variety of substrates and has a certain stability against protease and commercial washing powder,which has good potential on detergent and additive.