| Title : Purification and characterization of two distinct lipases from Geotrichum candidum - Veeraragavan_1990_Biochim.Biophys.Acta_1044_26 |
| Author(s) : Veeraragavan K , Colpitts T , Gibbs BF |
| Ref : Biochimica & Biophysica Acta , 1044 :26 , 1990 |
| Abstract : Lipase, an enzyme that hydrolyzes triacylglycerol, has been purified and characterized. The purification procedure includes ethanol precipitation and chromatographies on Sephacryl-200 HR, high resolution anion-exchange (mono Q) and Polybuffer exchanger 94. With this procedure, two forms of lipases from Geotrichum candidum were obtained. Lipase I (main enzyme) and lipase II (minor enzyme) were purified 35-fold with a 62% recovery in activity and 94-fold with a 18% recovery in activity, respectively. Their molecular weights have been estimated by polyacrylamide gel electrophoresis under denaturing conditions and by molecular sieving under native conditions at 56,000. Lipase I and II had optimum pH values of 6.0 and 6.8 and isoelectric points of 4.56 and 4.46, respectively. The enzymes are stable at a pH range of 6.0 to 8.0. Monovalent ions had little effect on both enzyme activities, while divalent ions at concentrations above 50 mM inhibited the lipase activities in a concentration-dependent manner. Sodium dodecyl sulfate at a concentration lower than 10 mM completely inhibited the lipase activity. |
| ESTHER : Veeraragavan_1990_Biochim.Biophys.Acta_1044_26 |
| PubMedSearch : Veeraragavan_1990_Biochim.Biophys.Acta_1044_26 |
| PubMedID: 2340308 |
Veeraragavan K, Colpitts T, Gibbs BF (1990)
Purification and characterization of two distinct lipases from Geotrichum candidum
Biochimica & Biophysica Acta
1044 :26
Veeraragavan K, Colpitts T, Gibbs BF (1990)
Biochimica & Biophysica Acta
1044 :26