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Contribution of sarcoplasmic proteins to myofibrillar proteins gelation

journal contribution
posted on 2024-11-01, 11:16 authored by Ali Jafarpour, Elisabeth Gorczyca
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

History

Journal

Journal of Food Science

Volume

77

Issue

2

Start page

R73

End page

R81

Total pages

9

Publisher

Wiley-Blackwell Publishing

Place published

United States

Language

English

Copyright

© 2012 Institute of Food Technologists

Former Identifier

2006033753

Esploro creation date

2020-06-22

Fedora creation date

2015-01-16

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