Contribution of Sarcoplasmic Proteins to Myofibrillar Proteins Gelation
Article first published online: 6 JAN 2012
© 2012 Institute of Food Technologists®
Journal of Food Science
Volume 77, Issue 2, pages R73–R81, February 2012
How to Cite
Jafarpour, A. and Gorczyca, E. M. (2012), Contribution of Sarcoplasmic Proteins to Myofibrillar Proteins Gelation. Journal of Food Science, 77: R73–R81. doi: 10.1111/j.1750-3841.2011.02521.x
- Issue published online: 17 FEB 2012
- Article first published online: 6 JAN 2012
- MS 20110589 Submitted 5/10/2011, Accepted 10/26/2011.
- gel strength;
- myofibrillar proteins;
- sarcoplasmic proteins;
Abstract: Surimi, a refined protein extract, is produced by solubilizing myofibrillar proteins during the comminuting and salting stages of manufacturing. The resulting paste gels on heating to produce kamaboko or a range of analog shellfish such as crab claw, filament sticks, fish mushroom, and so on. The myosin molecule is the major myofibrillar protein in gelation. It is believed that washing steps during the traditional surimi process play an important role in enhancing the gel properties of the resultant kamaboko by removing water-soluble (sarcoplasmic, Sp-P) proteins. By contrast, some researchers claim that retaining Sp-P or adding it into the surimi gel network not only does not interfere with the action of myofibrillar proteins during the sol–gel transition step but also improves the gel characteristics of the resultant kamaboko. It seems that retention of Sp-P or their addition into raw surimi does enhance the textural properties of kamaboko gel perhaps by functioning as a proteinase inhibitor, particularly against trypsin and trypsin-like proteinases but this depends on the type of applied surimi process. Among different types of Sp-P, it has been claimed that some proteins such as endogenous transglutaminase (TGase) play a more important role than other Sp-P in bond formation, by catalyzing the cross-linking of myosin heavy chain (MHC) molecules during low-temperature setting of surimi, resulting a more elastic kamaboko gel.