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Rapid heating of Alaska pollock and chicken breast myofibrillar proteins as affecting gel rheological properties.
J Food Sci. 2013 Jul; 78(7):C971-7.JF

Abstract

Surimi seafoods (fish/poikilotherm protein) in the U.S.A. are typically cooked rapidly to 90+°C, while comminuted products made from land animals (meat/homeotherm protein) are purposely cooked much more slowly, and to lower endpoint temperatures (near 70 °C). We studied heating rate (0.5, 25, or 90 °C/min) and endpoint temperature (45 to 90 °C) effects on rheological properties (fracture, small strain) of washed myofibril gels derived from fish (Alaska pollock) compared with chicken breast at a common pH (6.75). This was contrasted with published data on gelation kinetics of chicken myosin over the same temperature range. Heating rate had no effect on fracture properties of fish gels but slow heating did yield somewhat stronger, but not more deformable, chicken gels. Maximum gel strength by rapid heating could be achieved within 5 min holding after less than 1 min heating time. Dynamic testing by small strain revealed poor correspondence of the present data to that published for gelling response of chicken breast myosin in the same temperature range. The common practice of reporting small-strain rheological parameters measured at the endpoint temperature was also shown to be misleading, since upon cooling, there was much less difference in rigidity between rapidly and slowly heated gels for either species.

Authors+Show Affiliations

Department of Food, Bioprocessing and Nutrition Sciences, North Carolina State University, Raleigh, NC 27695, USA.No affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

23646872

Citation

Liu, Wenjie, et al. "Rapid Heating of Alaska Pollock and Chicken Breast Myofibrillar Proteins as Affecting Gel Rheological Properties." Journal of Food Science, vol. 78, no. 7, 2013, pp. C971-7.
Liu W, Stevenson CD, Lanier TC. Rapid heating of Alaska pollock and chicken breast myofibrillar proteins as affecting gel rheological properties. J Food Sci. 2013;78(7):C971-7.
Liu, W., Stevenson, C. D., & Lanier, T. C. (2013). Rapid heating of Alaska pollock and chicken breast myofibrillar proteins as affecting gel rheological properties. Journal of Food Science, 78(7), C971-7. https://doi.org/10.1111/1750-3841.12147
Liu W, Stevenson CD, Lanier TC. Rapid Heating of Alaska Pollock and Chicken Breast Myofibrillar Proteins as Affecting Gel Rheological Properties. J Food Sci. 2013;78(7):C971-7. PubMed PMID: 23646872.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Rapid heating of Alaska pollock and chicken breast myofibrillar proteins as affecting gel rheological properties. AU - Liu,Wenjie, AU - Stevenson,Clint D, AU - Lanier,Tyre C, Y1 - 2013/05/06/ PY - 2012/09/13/received PY - 2013/04/01/accepted PY - 2013/5/8/entrez PY - 2013/5/8/pubmed PY - 2014/2/12/medline KW - gelation KW - isothermal heating KW - myofibrillar protein KW - species KW - viscoelasticity SP - C971 EP - 7 JF - Journal of food science JO - J Food Sci VL - 78 IS - 7 N2 - Surimi seafoods (fish/poikilotherm protein) in the U.S.A. are typically cooked rapidly to 90+°C, while comminuted products made from land animals (meat/homeotherm protein) are purposely cooked much more slowly, and to lower endpoint temperatures (near 70 °C). We studied heating rate (0.5, 25, or 90 °C/min) and endpoint temperature (45 to 90 °C) effects on rheological properties (fracture, small strain) of washed myofibril gels derived from fish (Alaska pollock) compared with chicken breast at a common pH (6.75). This was contrasted with published data on gelation kinetics of chicken myosin over the same temperature range. Heating rate had no effect on fracture properties of fish gels but slow heating did yield somewhat stronger, but not more deformable, chicken gels. Maximum gel strength by rapid heating could be achieved within 5 min holding after less than 1 min heating time. Dynamic testing by small strain revealed poor correspondence of the present data to that published for gelling response of chicken breast myosin in the same temperature range. The common practice of reporting small-strain rheological parameters measured at the endpoint temperature was also shown to be misleading, since upon cooling, there was much less difference in rigidity between rapidly and slowly heated gels for either species. SN - 1750-3841 UR - https://www.unboundmedicine.com/medline/citation/23646872/Rapid_heating_of_Alaska_pollock_and_chicken_breast_myofibrillar_proteins_as_affecting_gel_rheological_properties_ L2 - https://doi.org/10.1111/1750-3841.12147 DB - PRIME DP - Unbound Medicine ER -