The lipolytic degradation of highly structured cubic micellar nanoparticles of soy phosphatidylcholine and glycerol dioleate by phospholipase A2 and triacylglycerol lipase

Maria Wadsäter, Justas Barauskas, Fredrik Tiberg, Tommy Nylander

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)86-92
JournalChemistry and Physics of Lipids
Volume211
Early online date2017 Nov 11
DOIs
Publication statusPublished - 2018

Subject classification (UKÄ)

  • Physical Chemistry (including Surface- and Colloid Chemistry)

Free keywords

  • Cryogenic transmission electron microscopy
  • Lipid liquid crystalline nano-particles
  • Lipolytic enzymes
  • Phospholipase A
  • Small angle X-ray diffraction
  • Triacylglycerol lipase

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