An improved method to measure lipase activity in aqueous media.

Autor: Hernández-García S; Department of Biochemistry and Molecular Biology-A, Faculty of Biology, Regional Campus of International Excellence 'Campus Mare Nostrum', University of Murcia, Campus Espinardo, E-30100 Murcia, Spain. Electronic address: samanta.hernandez@um.es., García-García MI; Department of Biochemistry and Molecular Biology-A, Faculty of Biology, Regional Campus of International Excellence 'Campus Mare Nostrum', University of Murcia, Campus Espinardo, E-30100 Murcia, Spain., García-Carmona F; Department of Biochemistry and Molecular Biology-A, Faculty of Biology, Regional Campus of International Excellence 'Campus Mare Nostrum', University of Murcia, Campus Espinardo, E-30100 Murcia, Spain.
Jazyk: angličtina
Zdroj: Analytical biochemistry [Anal Biochem] 2017 Aug 01; Vol. 530, pp. 104-106. Date of Electronic Publication: 2017 May 11.
DOI: 10.1016/j.ab.2017.05.012
Abstrakt: An improved method based on the p-nitrophenyl long chain esters method is proposed for measuring lipase hydrolytic activity in aqueous media. Using ethylene glycol as co-solvent for hydrophobic p-nitrophenyl substrates in aqueous buffer, lipase activity is measured by following the release of p-nitrophenol. This fast and easy to handle method improves the solubility of both substrate and product, and also the stability of the substrate. It avoids the use of solvents such as ethanol or propanol, permits the comparison of all the p-nitrophenol acyl ester substrates and allows the influence of ions like Ca +2 to be studied, while avoiding turbidity in the reaction medium.
(Copyright © 2017 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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