Ruiz_2001_Lipids_36_283

Reference

Title : Purification and characterization of an extracellular lipase from Penicillium candidum - Ruiz_2001_Lipids_36_283
Author(s) : Ruiz B , Farres A , Langley E , Masso F , Sanchez S
Ref : Lipids , 36 :283 , 2001
Abstract :

Penicillium candidum produces and secretes a single extracellular lipase with a monomer molecular weight of 29 kDa. However, this enzyme forms dimers and higher molecular weight aggregates under nondenaturing conditions. The lipase from P. candidum was purified 37-fold using Octyl-Sepharose CL-4B and DEAE-Sephadex columns. The optimal assay conditions for lipase activity were 35 degrees C and pH 9. The lipase was stable in the pH range of 5-6 with a pl of 5.5, but rapid loss of the enzyme activity was observed above 25 degrees C. Tributyrin was found to be the best substrate for the P. candidum lipase, among those tested. Metal ions such as Fe2+ and Cu2+ inhibited enzymatic activity and only Ca2+ was able to slightly enhance lipase activity. Ionic detergents inhibited the activity of the enzyme, whereas nonionic detergents stimulated lipase activity.

PubMedSearch : Ruiz_2001_Lipids_36_283
PubMedID: 11337984

Related information

Citations formats

Ruiz B, Farres A, Langley E, Masso F, Sanchez S (2001)
Purification and characterization of an extracellular lipase from Penicillium candidum
Lipids 36 :283

Ruiz B, Farres A, Langley E, Masso F, Sanchez S (2001)
Lipids 36 :283