Carrageenan Effects on Thermal Stability of Meat Proteins

Authors

  • Z. DeFREITAS,

    1. Authors DeFreitas, Sebranek and Olson are with the Depts. of Food Science & Human Nutrition and of Animal Science, Iowa State Univ., Ames, IA. Author Carr is with SBI Systems Bio-Industries, Inc., Waukesha, WI.
    Search for more papers by this author
  • J.G. SEBRANEK,

    1. Authors DeFreitas, Sebranek and Olson are with the Depts. of Food Science & Human Nutrition and of Animal Science, Iowa State Univ., Ames, IA. Author Carr is with SBI Systems Bio-Industries, Inc., Waukesha, WI.
    Search for more papers by this author
  • D.G. OLSON,

    1. Authors DeFreitas, Sebranek and Olson are with the Depts. of Food Science & Human Nutrition and of Animal Science, Iowa State Univ., Ames, IA. Author Carr is with SBI Systems Bio-Industries, Inc., Waukesha, WI.
    Search for more papers by this author
  • J.M. CARR

    1. Authors DeFreitas, Sebranek and Olson are with the Depts. of Food Science & Human Nutrition and of Animal Science, Iowa State Univ., Ames, IA. Author Carr is with SBI Systems Bio-Industries, Inc., Waukesha, WI.
    Search for more papers by this author

  • Journal Paper No. J-16465 of the Iowa Agriculture and Home Economics Experiment Station, Ames, IA. Project No. 2723.

ABSTRACT

Meat myofibrillar protein (MP) gels and ground pork were used as model systems for studying thermal transition temperatures. Addition of up 2% of κ, ι, or λ carrageenan (CGN) to MP caused a very slight change in the thermal denaturation of the meat proteins. Three transition temperatures were found in ground pork samples, which were characteristic of myosin (59.4°C), sarcoplasmic proteins (67.8°C), and actin (82.4°C). Mixtures of high ionic strength had lower thermal transition peaks. CGN did not cause major shifts in transition temperatures, suggesting that molecular interactions between CGN and meat proteins did not occur.

Ancillary