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• W2006591992 abstract "Lipase from Pseudomonas fluorescens (PFL), an enzyme with a great tendency to yield bimolecular aggregates, was immobilized via multipoint covalent attachment on glyoxyl-agarose in the presence of Triton X-100. This strategy permitted to obtain the enzyme with the active center oriented towards the reaction medium. This immobilized enzyme presents the capacity of specifically adsorbing PFL molecules, that can be easily desorbed by the use of detergents. More interesting, the enzyme was also able to adsorb other lipases. That is, the lipase from Bacillus thermocatenulatus (BTL2) cloned in Escherichia coli was selectively adsorbed on this immobilized enzyme, enabling a very simple purification strategy. Similar results were achieved with some other lipases (those from Rhizomucor miehei (RML), Rhizopus oryzae (ROL), and Humicola Lanuginosa (HLL)). In all cases, the enzyme could be easily desorbed by incubation with Triton X-100. The matrix could be used several cycles without any detrimental effect on the adsorption capacity." @default.
• W2006591992 created "2016-06-24" @default.
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• W2006591992 date "2004-06-01" @default.
• W2006591992 modified "2023-10-08" @default.
• W2006591992 title "Use of immobilized lipases for lipase purification via specific lipase–lipase interactions" @default.
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• W2006591992 doi "https://doi.org/10.1016/j.chroma.2004.03.058" @default.
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