rdf-syntax-grammar
mods:
  schema location: http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-2.xsd
  title info:
    non sort: A
    title: rheological characterization of heat-induced protein gels
  name:
    name part: Hickson, David Wayne.
    role:
      role term: creator
  name:
    name part: Carpenter, Z. L.
    role:
      role term: degree committee member.
  name:
    name part: Dill, C. W.
    role:
      role term: degree supervisor.
  name:
    name part: Landmann, W. A.
    role:
      role term: degree committee member.
  name:
    name part: Sutar, D. A.
    role:
      role term: degree committee member.
  name:
    name part: Texas A & M University
    role:
      role term: degree granting institution.
  type of resource: text
  genre: bibliography
  genre: Academic theses.
  origin info:
    place:
      place term: xx
    date issued: 1981
    issuance: monographic
  language:
    language term: eng
  physical description:
    form: print
    extent: xiii, 121 leaves : illustrations ; 29 cm
  abstract: The purpose of this study was to develop and utilize models for assessing viscosity, elasticity and gel strength of heat-induced gels from bovine plasma protein and egg albumen and to characterize the rheological response of these proteins when subjected to heat treatments and adjustments in pH and salt concentration. The counter-flow back-extrusion method, and the developed equations, sensitively measured rheological differences occurring between 8% protein suspensions of heat-induced (80(DEGREES)C) gels of bovine plasma protein and egg albumen. Bovine plasma protein consistently produced significantly greater rheological responses than egg albumen. Interactions between NaCl concentration, pH and heating temperature on the rheological properties of 8 and 10% bovine plasma protein gels heated for 60 min were not significant. The main effects, temperature and pH, were consistently significant and seemed to have an additive effect on the rheological properties. Sodium chloride concentration was not a significant effect. pH changes during storage of egg albumen produced a marked effect on the heat-induced rheological properties of this protein system. Egg albumen stored as whole eggs increased in pH to a value of 9.0 in 5 days of storage at 15(DEGREES)C, whereas semipermeable membrane stored eggs never attained a pH of 9.0. Egg albumen stored as whole eggs reached a much higher elasticity level and gel strength than eggs stored in semipermeable membranes. Viscosity levels remained the same in egg albumen stored in the two methods. Thin albumen produced significantly greater viscosity than thick albumen at the 0 day of storage, but this effect was masked at the longer storage periods because of pH changes.
  note: "Major subject: Food Science and Technology."
  note: Typescript (photocopy).
  note: Vita.
  note: Ph. D. in Philosophy Texas A & M University 1981
  note: Includes bibliographical references (leaves 113-120).
  subject:
    topic: Food texture
  subject:
    topic: Polymerization
  subject:
    topic: Polymers
  subject:
    topic: Protein binding
  subject:
    topic: Rheology
  subject:
    topic: Food Science and Technology
  identifier: http://proxy.library.tamu.edu/login
  identifier: https://hdl.handle.net/1969.1/DISSERTATIONS-94424
  related item:
    location:
      url: https://hdl.handle.net/1969.1/DISSERTATIONS-94424
  record info:
    record content source: TXA
    record creation date: 820922
    record change date: 20220104090818.0
    record identifier: in00000086734
    language of cataloging:
      language term: eng