A Novel Low-Temperature Alkaline Lipase from Acinetobacter johnsonii LP28 Suitable for Detergent Formulation

摘要: Summary A strain LP28 that produces alkaline and low-temperature lipase was isolated from the soil collected Bay of Bohai, PR China identified as Acinetobacter johnsonii using 16S rDNA sequencing. The purified to homogeneity by centrifugation, followed ammonium sulphate precipitation, dialysis, ion exchange chromatography on cellulose DE-52 gel filtration Sephadex G-75. enzyme about 34-fold with a final yield 13 % relative molecular mass determined be 53 kDa SDS-PAGE. exhibited maximum activity at 30 °C pH=9.0, retained 94.53 its 20 °C. stable 50 80.9 original for min. It also highly in pH range 8.0–11.0. hydrolyzed wide oils showed high level hydrolyzing tributyrin. promoted presence Na + ,C 2+ ,K ,M g sodium citrate. Ba n , Cr 3+ Co did not affect activity, whereas Al u ,F e Fe ,Z EDTA reduced activity. Regarding stability detergent process, various oxidizing agents, some commercial detergents protease, most surfactants, viz. Tween 20, 80, cholate, taurocholate saponin. For these characteristics, good potential an additive laundry formulation.