A rheological characterization of heat-induced protein gels.

Bibliographic Details
Main Author: Hickson, David Wayne
Other Authors: Carpenter, Z. L. (degree committee member.), Landmann, W. A. (degree committee member.), Sutar, D. A. (degree committee member.)
Format: Thesis Book
Language:English
Published: 1981.
Subjects:
Online Access:Link to ProQuest Copy
Link to OAKTrust copy

MARC

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049 |a TXAM 
099 |a 1981  |a Dissertation  |a H631 
100 1 |a Hickson, David Wayne. 
245 1 2 |a A rheological characterization of heat-induced protein gels. 
264 1 |c 1981. 
300 |a xiii, 121 leaves :  |b illustrations ;  |c 29 cm 
336 |a text  |b txt  |2 rdacontent 
337 |a unmediated  |b n  |2 rdamedia 
338 |a volume  |b nc  |2 rdacarrier 
500 |a "Major subject: Food Science and Technology." 
500 |a Typescript (photocopy). 
500 |a Vita. 
502 |b Ph. D. in Philosophy  |c Texas A & M University  |d 1981 
504 |a Includes bibliographical references (leaves 113-120). 
520 3 |a 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. 
650 0 |a Food texture.  |0 http://id.loc.gov/authorities/subjects/sh85050345 
650 0 |a Polymerization.  |0 http://id.loc.gov/authorities/subjects/sh89001625 
650 0 |a Polymers.  |0 http://id.loc.gov/authorities/subjects/sh85104660 
650 0 |a Protein binding.  |0 http://id.loc.gov/authorities/subjects/sh85107654 
650 0 |a Rheology.  |0 http://id.loc.gov/authorities/subjects/sh85113619 
650 4 |a Food Science and Technology. 
655 7 |a Academic theses.  |2 lcgft  |0 http://id.loc.gov/authorities/genreForms/gf2014026039 
700 1 |a Carpenter, Z. L.,  |e degree committee member.  |0 http://id.loc.gov/authorities/names/no2018132577 
700 1 |a Dill, C. W.,  |e degree supervisor. 
700 1 |a Landmann, W. A.,  |e degree committee member. 
700 1 |a Sutar, D. A.,  |e degree committee member. 
710 2 |a Texas A & M University,  |e degree granting institution.  |0 http://id.loc.gov/authorities/names/n80125885 
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952 f f |p noncirc  |a Texas A&M University  |b J.J. Pickle Campus  |c High Density Repository  |d Remote Storage  |t 0  |e 1981 Dissertation H631  |h Other scheme  |i unmediated -- volume  |m A14841004890 
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