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      Screening and characterization of a novel alkaline lipase from Acinetobacter calcoaceticus 1-7 isolated from Bohai Bay in China for detergent formulation

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          Abstract

          A novel alkaline lipase-producing strain 1-7 identified as Acinetobacter calcoaceticus was isolated from soil samples collected from Bohai Bay, China, using an olive oil alkaline plate, which contained olive oil as the sole carbon source. The lipase from strain 1-7 showed the maximum activity at pH 9.0 under 40ºC. One interesting feature of this enzyme is that it exhibits lipase activity over a broad range of temperatures and good stability. It is also stable at a broad range of pHs from 4.0 to 10.0 for 24 h. Its catalytic activity was highly enhanced in the presence of Ca2+, Mg2+ and K+, but partially inhibited by Cu2+, Al3+, Fe3+ , Ba2+and Zn2+. The fact that it displays marked stability and activity in the presence of TritonX-100, Tween-20, Tween-80, SDS, Hydrogen peroxide, Sodium perborate, Sodium hypochlorite, Sodium citrate, Sodium taurocholate, Glycerine and NaCl suggests that this lipase is suitable as an additive in detergent formulations.

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          Screening, purification and properties of a thermophilic lipase from Bacillus thermocatenulatus.

          By screening of 15 thermophilic Bacillus strains, five strains exhibiting lipase activity were found. Among these the strain Bacillus thermocatenulatus (DSM 730) produced the highest lipase activity. The lipase proved to be inducible and extracellular and was purified 67-fold to homogenous state by hexane extraction, methanol precipitation and ion-exchange chromatography on Q-Sepharose. The molecular weight of the lipase determined by SDS-PAGE is 16 kDa. However, the lipase forms very large aggregates (> 750 kDa) as observed after native PAGE, which makes handling of the lipase very difficult. The lipase binds almost irreversibly on different chromatography matrices, e.g., Amberlite and Serolite, and is very stable in the immobilised form. The N-terminal sequence consists of 53% apolar amino acids and shows no significant homology towards other known lipase sequences. Maximum activity was found at pH 7.5-8.0 and 60-70 degrees C with pNPP and olive oil as substrates.
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            A noval thermostable lipasse from thermophilic Bacillus sp.: characterization and esterification studies

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              Production of an alkaline lipase by Acinetobacter radioresistens

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                Author and article information

                Contributors
                Role: ND
                Role: ND
                Role: ND
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                Role: ND
                Journal
                bjm
                Brazilian Journal of Microbiology
                Braz. J. Microbiol.
                Sociedade Brasileira de Microbiologia (São Paulo )
                1678-4405
                March 2012
                : 43
                : 1
                : 148-156
                Article
                S1517-83822012000100016
                10.1590/S1517-83822012000100016
                49ee5918-7a70-4532-96a9-a778df03f898

                http://creativecommons.org/licenses/by/4.0/

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                SciELO Brazil

                Self URI (journal page): http://www.scielo.br/scielo.php?script=sci_serial&pid=1517-8382&lng=en
                Categories
                MICROBIOLOGY

                Microbiology & Virology
                alkaline lipase,acinetobacter calcoaceticus,characterization,detergent
                Microbiology & Virology
                alkaline lipase, acinetobacter calcoaceticus, characterization, detergent

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