An active-site titration method for lipases
2000 (English)In: Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids, ISSN 1388-1981, E-ISSN 1388-1918, Vol. 1483, no 1, 132-140 p.Article in journal (Refereed) Published
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, 132-140 p.
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
IdentifiersURN: urn:nbn:se:kth:diva-19474ISI: 000084637100011OAI: oai:DiVA.org:kth-19474DiVA: diva2:338166
QC 201005252010-08-102010-08-10Bibliographically approved