2017
DOI: 10.1016/j.fbio.2016.11.001
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Gelation properties of tilapia fish protein isolate and surimi pre- and post-rigor

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Cited by 26 publications
(15 citation statements)
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“…The G ′ value of alkaline processed protein gel increased with an increase in temperature reaching a maximum at 70 °C, indicating a stable gel network. Kobayashi et al . and Kobayashi and Park also observed similar results.…”
Section: Resultssupporting
confidence: 67%
See 3 more Smart Citations
“…The G ′ value of alkaline processed protein gel increased with an increase in temperature reaching a maximum at 70 °C, indicating a stable gel network. Kobayashi et al . and Kobayashi and Park also observed similar results.…”
Section: Resultssupporting
confidence: 67%
“…32 The G ′ value of alkaline processed protein gel increased with an increase in temperature reaching a maximum at 70 ∘ C, indicating a stable gel network. Kobayashi et al 20 and Kobayashi and Park 32 also observed similar results. The G ′ value of acid processed isolate gel showed a decreasing trend with increasing temperature, which is not in agreement with earlier reports.…”
Section: Rheological Propertiessupporting
confidence: 54%
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“…Oscillatory rheometry and small-strain analysis using small amplitude oscillatory shear (SAOS) techniques can be used to determine the nonfracture mechanical properties based on viscous modulus (G") and elastic modulus (G'), which are 'finger prints' reflecting structural changes during gelation, while large-strain analysis including fracture analyses, such as texture profile analysis (TPA), torsion test, and ring tensile and punch tests of gel mechanical properties are correlated with sensory characteristics of surimi-based seafood products. Small-strain analysis has been widely used to elucidate the gelation mechanism of fish myofibrillar protein, i.e., the primary protein in surimi contributing to the texture properties of surimi seafood product [2][3][4].…”
Section: Introductionmentioning
confidence: 99%