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An active-site titration method for lipases
KTH, Superseded Departments, Biochemistry and Biotechnology.
KTH, Superseded Departments, Biochemistry and Biotechnology.ORCID iD: 0000-0002-2993-9375
2000 (English)In: Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids, ISSN 1388-1981, E-ISSN 1879-2618, Vol. 1483, no 1, p. 132-140Article in journal (Refereed) Published
Abstract [en]

A method for active-site titration of lipases has been developed based on irreversible inhibition by methyl p-nitrophenyl n-hexylphosphonate. This method was applied to five lipases displaying from minor to pronounced interfacial activation. Soluble and immobilized lipases were successfully titrated in aqueous media. A low concentration of sodium dodecyl sulfate was needed for lipases displaying pronounced interfacial activation. The carrier of some of the immobilized preparations adsorbed part of the produced p-nitrophenolate, This problem could be solved by extracting the p-nitrophenolate after inhibition. The method was extended to apolar organic solvents in the case of immobilized lipase preparations.

Place, publisher, year, edition, pages
2000. Vol. 1483, no 1, p. 132-140
Keyword [en]
concentration, immobilized lipase, aqueous medium, organic medium, interfacial activation, detergent, inhibitor, serine proteases, interfacial activation, organic-chemistry, in-vitro, biocatalysts, inhibition, solvents, cutinase, titrant, enzymes
Identifiers
URN: urn:nbn:se:kth:diva-19474ISI: 000084637100011OAI: oai:DiVA.org:kth-19474DiVA: diva2:338166
Note
QC 20100525Available from: 2010-08-10 Created: 2010-08-10 Last updated: 2017-12-12Bibliographically approved

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Martinelle, Mats

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