Purification and characterization of lipase from Acinetobacter haemolyticus TA 106 isolated from human skin
نویسندگان
چکیده
Acinetobacter sp. isolated from healthy human skin of a tribal population was tested for lipase production.Medium optimization was achieved to increase the production. Purification was carried out by a one-step purification process using DEAE Sephadex A-50. The molecular weight of the lipase was approximately 60 kDa by SDS-PAGE. The purified lipase showed not only good stability in the presence of detergents and organic solvents but also an enhancement of activity. The lipase was active at pH 9 and displayed good activity at 0, 30 and 37°C. It was inhibited in EDTA, suggesting that it is a metalloenzyme. The cations like Ca, Mg, and Cu significantly reduced the lipase activity at 5 mM concentration. The lipase converted 67% oleic acid to methyl oleate at 37°C at 72 h. All these features make this lipase an important candidate from an industrial point of view.
منابع مشابه
Optimization of medium for lipase production by Acinetobacter haemolyticus from healthy human skin.
A lipase producing Acinetobacter haemolyticus TA106 was isolated from healthy human skin of tribal population. The maximum activity of 55 U/ml was observed after medium optimization using the "one variable at a time" and the statistical approaches. The optimal composition of the medium was determined as (% w/v or v/v): tryptone--1, yeast extract--0.5, sodium chloride-1, olive oil-1, Tween-80 1,...
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