Effects of thermal sensitivity of fish proteins from various species on rheological properties of gels

O. Esturk; J. W. Park; S. Thawornchinsombut

doi:10.1111/j.1750-3841.2004.tb18017.x

Effects of thermal sensitivity of fish proteins from various species on rheological properties of gels

O. Esturk, J. W. Park^*, S. Thawornchinsombut

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

28 Citations (Scopus)

Abstract

Thermal sensitivity of myofibrillar proteins from various fish species were compared at various pre-incubation (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.

Original language	English
Pages (from-to)	E412-E416
Journal	Journal of Food Science
Volume	69
Issue number	8
DOIs	https://doi.org/10.1111/j.1750-3841.2004.tb18017.x
Publication status	Published - 2004 Oct

Keywords

Rheology
Setting
Thermal sensitivity
Warm-water fish

ASJC Scopus subject areas

Food Science

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10.1111/j.1750-3841.2004.tb18017.x

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title = "Effects of thermal sensitivity of fish proteins from various species on rheological properties of gels",

abstract = "Thermal sensitivity of myofibrillar proteins from various fish species were compared at various pre-incubation (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.",

keywords = "Rheology, Setting, Thermal sensitivity, Warm-water fish",

author = "O. Esturk and Park, \{J. W.\} and S. Thawornchinsombut",

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language = "English",

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AU - Esturk, O.

AU - Park, J. W.

AU - Thawornchinsombut, S.

PY - 2004/10

Y1 - 2004/10

N2 - Thermal sensitivity of myofibrillar proteins from various fish species were compared at various pre-incubation (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.

AB - Thermal sensitivity of myofibrillar proteins from various fish species were compared at various pre-incubation (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.

KW - Rheology

KW - Setting

KW - Thermal sensitivity

KW - Warm-water fish

UR - https://www.scopus.com/pages/publications/7444239069

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DO - 10.1111/j.1750-3841.2004.tb18017.x

M3 - Article

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SN - 0022-1147

VL - 69

SP - E412-E416

JO - Journal of Food Science

JF - Journal of Food Science

IS - 8

ER -

Effects of thermal sensitivity of fish proteins from various species on rheological properties of gels

Abstract

Keywords

ASJC Scopus subject areas

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