Wadsater_2018_Chem.Phys.Lipids_211_86

Reference

Title : The lipolytic degradation of highly structured cubic micellar nanoparticles of soy phosphatidylcholine and glycerol dioleate by phospholipase A2 and triacylglycerol lipase - Wadsater_2018_Chem.Phys.Lipids_211_86
Author(s) : Wadsater M , Barauskas J , Tiberg F , Nylander T
Ref : Chemistry & Physic of Lipids , 211 :86 , 2018
Abstract :

The effects of different lipolytic enzymes on the structure of lipid liquid crystalline nano-particles (LCNP) have been investigated by cryogenic transmission electron microscopy (cryo-TEM) and synchrotron small angle X-ray diffraction (SAXD). Here we used highly structured cubic micellar (Fd3m) nanoparticles of 50/50 (wt%/wt%) soy phosphatidyl choline (SPC)/glycerol dioleate (GDO) as substrate. Two types of lipolytic enzymes were used, phospholipase A2 (PLA2) that catalyses degradation of the phospholipid component, SPC, and porcine pancreatic triacylglycerol lipase (TGL) that facilitate the hydrolysis of the diglyceride, GDO. Evolution of the structure was found to be very different and linked to specificity of the two types of enzymes. PLA2, which hydrolyses the lamellar forming component, SPC, induces a reversed micellar lipid phase, while TGL which hydrolysis the reverse phase forming compound, GDO, induces a lamellar phase.

PubMedSearch : Wadsater_2018_Chem.Phys.Lipids_211_86
PubMedID: 29132829

Related information

Substrate 1,2-Diolein

Citations formats

Wadsater M, Barauskas J, Tiberg F, Nylander T (2018)
The lipolytic degradation of highly structured cubic micellar nanoparticles of soy phosphatidylcholine and glycerol dioleate by phospholipase A2 and triacylglycerol lipase
Chemistry & Physic of Lipids 211 :86

Wadsater M, Barauskas J, Tiberg F, Nylander T (2018)
Chemistry & Physic of Lipids 211 :86