Title : An active-site titration method for lipases - Rotticci_2000_Biochim.Biophys.Acta_1483_132
Author(s) : Rotticci D , Norin T , Hult K , Martinelle M
Ref : Biochimica & Biophysica Acta , 1483 :132 , 2000
Abstract :

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.

PubMedSearch : Rotticci_2000_Biochim.Biophys.Acta_1483_132
PubMedID: 10601702

Related information

Inhibitor M4-4NHP

Citations formats

Rotticci D, Norin T, Hult K, Martinelle M (2000)
An active-site titration method for lipases
Biochimica & Biophysica Acta 1483 :132

Rotticci D, Norin T, Hult K, Martinelle M (2000)
Biochimica & Biophysica Acta 1483 :132