Neutron diffraction of deuterated tripalmitin and the influence of shear on its crystallisation
| Autor: | Helen E. Maynard-Casely, A.E. Leung, Barbara H. Stuart, Paul S. Thomas, Norman Booth |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Diffraction
030303 biophysics Neutron diffraction Biophysics Palmitic Acid Analytical chemistry Biochemistry law.invention Physics::Fluid Dynamics 03 medical and health sciences Crystallinity chemistry.chemical_compound Rheology law Crystallization Molecular Biology Triglycerides 030304 developmental biology 0303 health sciences Molecular Structure Chemistry Organic Chemistry Cell Biology Condensed Matter::Soft Condensed Matter Shear rate Neutron Diffraction Shear (geology) Tripalmitin |
| Zdroj: | Chemistry and Physics of Lipids. 221:108-113 |
| ISSN: | 0009-3084 |
| DOI: | 10.1016/j.chemphyslip.2019.02.011 |
| Popis: | © 2019 This neutron diffraction study of deuterated tripalmitin has provided further insight into a forensic observation of the crystallisation of lipids under high-shear conditions. To achieve this, an experimental set up was designed to enable simultaneous rheological data from a Couette cell to be recorded with neutron powder diffraction, enabling the influence of shear on the polymorph transformation on cooling to be monitored in real time. Tripalmitin was observed to directly transform from a liquid phase to a β polymorph under the influence of shear. Although the liquid to β transition was not observed to be influenced by shear rate, the degree of crystallinity, qualitatively denoted by an increase in the sharpness of the diffraction peaks, was observed at higher shear rates. Evidence is also presented that the rate of cooling influences the ordering in the β-polymorph produced in zero shear conditions. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect