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The use of detergent‐based aqueous two‐phase systems for the isolation of extracellular proteins: purification of a lipase from Pseudomonas cepacia
Author(s) -
Terstappen GC,
Geerts AJ,
Kula MR
Publication year - 1992
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1992.tb00225.x
Subject(s) - lipase , coacervate , extracellular , pseudomonas , triacylglycerol lipase , chromatography , chemistry , biochemistry , pseudomonadaceae , aqueous two phase system , bacteria , enzyme , aqueous solution , biology , organic chemistry , genetics
The partitioning of a variety of extracellular lipases, both pro‐ and eucaryotic, in detergent‐based aqueous two‐phase systems was examined. The results revealed that all procaryotic lipases showed a clear preference for the detergent‐rich coacervate phase. In contrast, all eucaryotic lipases were significantly excluded from this phase, most probably caused by their glycosylation. The potential of such detergent‐based systems for the isolation of extracellular lipases directly from cell‐free culture broth was analyzed using the bacterium Pseudomonas cepacia (DSM 50181). This strain was identified after a limited screening for lipase activity. About 76% of the lipase could be extracted into the coacervate phase in just one purification step, leading to a four‐fold concentration of lipase and a purification factor of 24.