Get access

Rheological Properties of Two Heat-Induced Protein Gels

Authors

  • D. W. HICKSON,

    1. Author Hickson is with the Food Science Institute of Union Carbide, Chicago, IL.
    Search for more papers by this author
  • C. W. DILL,

    1. Authors Dill and Carpenter are with the Animal Science Dept. and authors Suter and Sweat are with the Agricultural Engineering Dept., Texas A&M Univ., College Station, TX 77843.
    Search for more papers by this author
  • R. G. MORGAN,

    1. Author Morgan is with Corporate Research & Development, Ralston Purina Co., St. Louis, MO.
    Search for more papers by this author
  • V. E. SWEAT,

    1. Authors Dill and Carpenter are with the Animal Science Dept. and authors Suter and Sweat are with the Agricultural Engineering Dept., Texas A&M Univ., College Station, TX 77843.
    Search for more papers by this author
  • D. A. SUTER,

    1. Authors Dill and Carpenter are with the Animal Science Dept. and authors Suter and Sweat are with the Agricultural Engineering Dept., Texas A&M Univ., College Station, TX 77843.
    Search for more papers by this author
  • Z. L. CARPENTER

    1. Authors Dill and Carpenter are with the Animal Science Dept. and authors Suter and Sweat are with the Agricultural Engineering Dept., Texas A&M Univ., College Station, TX 77843.
    Search for more papers by this author

  • Technical Article No. TA-16902 of the Texas Agricultural Experiment Station. this work was supported in part by the Houston Livestock Show and Rodeo Association.

ABSTRACT

Rheological properties of heat-induced gels from egg albumen and bovine plasma proteins were measured using a mechanical loading device. Each protein was tested at 8% protein concentration and heated for 0–120 min at 80°C in an agitating water bath. After heating, the viscosity index, apparent elasticity and initial penetration force of the gels were evaluated. Bovine plasma protein dispersions exhibited a substantially higher viscosity index, apparent elasticity and initial penetration force than egg albumen gels. Bovine plasma proteins produced a gel structure which was strong and elastic. By comparison, heat-induced gels of egg albumen proteins were fragile and somewhat brittle.

Ancillary