부산대학교 도서관

Hypothesis Oleosomes are stabilized by a complex outer phospholipid-protein-layer. To improve understanding of its structure and stabilization mechanism, this shell has to be studied in extracellular native conditions. This should be possible by SANS using contrast variation. Oleosomes are expected to be highly temperature stable, with molecular changes occurring first in the protein shell. Direct measurements of changes in the shell structure are also important for processing methods, e.g. encapsulation. Experiments Extracted soybean oleosomes were studied directly and after encapsulation with pectin by SANS using contrast variation. In order to determine structure and size, a shell model of oleosomes was developed. The method was tested against a simple phospholipid-stabilized emulsion. The oleosomes’ temperature stability was investigated by performing SANS at elevated temperatures. Findings Size ( R g  = 1380 Å) and shell thickness of native and encapsulated oleosomes have been determined. This is the first report measuring the shell thickness of oleosomes directly. For native oleosomes, a shell of 9 nm thickness surrounds the oil core, corresponding to a layer of phospholipids and proteins. Up to 90 °C, no structural change was observed, confirming the oleosomes’ high temperature stability. Successful coavervation of oleosomes was shown by an increase in shell thickness of 10 nm after electrostatic deposition of pectin. [ABSTRACT FROM AUTHOR]