Single-step purification of different lipases from Staphylococcus warneri
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Updated: Jun 18, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Giandra Volpato1, Marco Filice, Marco A Z Ayub
1Departamento de Biocatalisis, Instituto de Catalisis (CSIC), Madrid, Spain.
Abstract:
Three different lipases from the extract crude of Staphylococcus warneri have been purified by specific lipase-lipase interactions using different lipases (TLL, RML, PFL, BTL2) covalently attached to a solid support as adsorption matrix. BTL2 immobilized on glyoxyl-DTT adsorbed selectivity only a 30 kDa lipase from the crude, which was desorbed by adding 0.1% triton X-100. Using glyoxyl-PFL as matrix, two new lipases (28 and 40 kDa) were adsorbed, and completely pure 40 kDa lipase was obtained after desorption using 0.01% triton, whereas 28 kDa lipase was desorbed after the incubation of the lipase matrix with 3% detergent. When using other matrixes as glyoxyl-TLL or glyoxyl-RML, different lipases were adsorbed. This methodology could be a very efficient and useful method to purify several lipases from crude extracts from different sources.

