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The lipolytic degradation of highly structured cubic micellar nanoparticles of soy phosphatidylcholine and glycerol dioleate by phospholipase A and triacylglycerol lipase.
Physical Chemistry, Department of Chemistry, Lund University, P.O. Box 124, SE-22100, Lund, Sweden.
Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Camurus AB , Ideon Science Park, Gamma Building, Sölvegatan 41, SE-22379 Lund, Sweden.
Physical Chemistry, Department of Chemistry, Lund University, P.O. Box 124, SE-22100, Lund, Sweden; Camurus AB, Ideon Science Park, Gamma Building, Sölvegatan 41, SE-22379, Lund, Sweden(1).
Physical Chemistry, Department of Chemistry, Lund University, P.O. Box 124, SE-22100, Lund, Sweden.
2018 (English)In: Chemistry and Physics of Lipids, ISSN 0009-3084, E-ISSN 1873-2941, Vol. 211, p. 86-92Article in journal (Refereed)
Abstract [en]

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 A (PLA) 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. PLA, 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.

Place, publisher, year, edition, pages
Elsevier, 2018. Vol. 211, p. 86-92
Keywords [en]
Cryogenic transmission electron microscopy, Lipid liquid crystalline nano-particles, Lipolytic enzymes, Phospholipase A(2), Small angle X-ray diffraction, Triacylglycerol lipase
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:mau:diva-4828DOI: 10.1016/j.chemphyslip.2017.11.011ISI: 000428484800010PubMedID: 29132829Scopus ID: 2-s2.0-85034242000Local ID: 25813OAI: oai:DiVA.org:mau-4828DiVA, id: diva2:1401662
Available from: 2020-02-28 Created: 2020-02-28 Last updated: 2024-06-17Bibliographically approved

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Barauskas, Justas

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