Kinetics and stability of a Chromobacterium viscosum lipase in reversed micellar and aqueous media.
The lipolytic activity of Chromobacterium viscosum lipase B (EC 3.1.1.3.; triacylglycerol hydrolase) solubilized both in water and AOT/isooctane reversed micelles has been investigated using triolein as a substrate. The influence of relevant parameters in the catalytic activity such as temperature, pH, surfactant and substrate concentrations, and water content was tested and compared in both media. A study of stability of the lipase was carried out, with particular reference to the influence of pH. Three major effects of the encapsulation of the lipase in the micelles were observed: increased activity (up to 7 times higher than in water), greater stability, specially at pH 7, and higher resistance to thermal deactivation.
Laboratório de Engenharia Bioquímica, Instituto Superior Técnico, Lisboa, Portugal.
D M
DM
Prazeres
F A
FA
Garcia
J M
JM
Cabral
D002861:Chromobacterium / Q000201:enzymology*; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D008823:Micelles; D012996:Solutions; D013379:Substrate Specificity; D013696:Temperature; D014304:Triolein; D014867:Water
D008823:Micelles; D012996:Solutions; D014867:Water; D014304:Triolein; D008049:Lipase