Characterization of heat-induced aggregates of globulin from common buckwheat (Fagopyrum esculentum Moench)

Document Type

Journal Article

Publication Date

2006

Keywords

Fagopyrum esculentum moench, Buckwheat globulin, Thermal aggregation, Transmission electron microscopy

DOI

10.1016/j.ijbiomac.2006.03.025

Abstract

Some physicochemical properties and the microstructure of heat-induced aggregates of globulin from common buckwheat (Fagopyrum esculentum Moench) (BWG) formed at 100 °C in 0.01 M phosphate buffer containing 1.0 M NaCl, pH 7.4 were studied. Differential scanning calorimetric (DSC) analysis shows a re-distribution of native and extensively denatured proteins in the heat-induced aggregates of BWG, particularly in the ISA fraction. Sodium dodecyl sulfate polyacrylamide gel electrophoretic (SDS-PAGE) analysis suggests the occurrence of both dissociation and association of molecules and the involvement of intermolecular disulfide linkages during thermal aggregation. Transmission electron microscopy (TEM) reveals that native BWG appeared as uniform compact globules with diameters ranging between 11.7 and 12.5 nm. TEM examination of the buffer-soluble aggregates, fractionated by sucrose density gradient ultracentrifugation, demonstrates the formation of strand-like small aggregates and large compact globular soluble macroaggregates.

Source Publication

International Journal of Biological Macromolecules

Volume Number

39

Issue Number

4-5

First Page

201

Last Page

209

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