Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1190658 | Food Chemistry | 2010 | 7 Pages |
The types of interactions and the proteins involved in the formation of gel network of fermented silver carp mince were investigated. Results showed that the amount of each type of protein interactions varied significantly depending on fermentation time. The content of sulphydryl groups decreased continually with a concomitant increase in disulphide bonds during fermentation. The higher gel strength and more compact fibrous network of fermented silver carp mince corresponded to a higher percentage of hydrophobic interactions, disulphide bonds and non-disulphide covalent bonds. SDS–PAGE showed that the major myofibrillar proteins, particularly myosin heavy chain were involved in the formation of aggregates through hydrophobic interactions and disulphide bonds during fermentation. Furthermore, low molecular weight proteins probably produced by proteolysis were also involved in the formation of gel matrix.