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Effects of Thermal Sensitivity of Fish Proteins from Various Species on Rheological Properties of Gels
Author(s) -
Esturk O.,
Park J.W.,
Thawornchinsombut S.
Publication year - 2004
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1750-3841.2004.tb18017.x
Subject(s) - myofibril , chemistry , rheology , myosin , fish <actinopterygii> , thermal stability , food science , incubation , biology , fishery , materials science , biochemistry , composite material , organic chemistry
Thermal sensitivity of myofibrillar proteins from various fish species were compared at various preincubation (setting) treatments and chopping temperatures. There was a significant species effect on gel texture by both pre‐incubation and chopping temperatures. Whereas Alaska pollock had the highest shear stress values at 5 °C or lower temperatures, big eye, lizardfish, and threadfin bream had higher fracture shear stress values at 25 °C or higher temperatures. Decreased intensity of myosin heavy chain (MHC) for warm‐water species set at 40 °C clearly revealed higher thermal stability of these particular species.