Influence of salts on the microstructural and rheological properties of heat-induced protein networks from ovalbumin and vicilin
- 1 June 1990
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of Agricultural and Food Chemistry
- Vol. 38 (6) , 1335-1343
- https://doi.org/10.1021/jf00096a008
Abstract
No abstract availableThis publication has 18 references indexed in Scilit:
- Role of the Thermal Denaturation-Aggregation Relationship in Determining the Rheological Properties of Heat Induced Networks for Ovalbumin and VicilinJournal of Food Science, 1989
- Forces Involved in Soy Protein Gelation: Effects of Various Reagents on the Formation, Hardness and Solubility of Heat‐Induced Gels Made from 7S, 11S, and Soy IsolateJournal of Food Science, 1985
- A Comparison Between Ovalbumin Gels Formed by Heat and by Guanidinium Hydrochloride DenaturationJournal of Food Science, 1984
- Correlation of the Rheological Behavior of Egg Albumen to Temperature, pH, and NaCl ConcentrationJournal of Food Science, 1984
- Effects of various anions on the rheological and gelling behavior of soy proteins: thermodynamic observationsJournal of Agricultural and Food Chemistry, 1983
- Effects of Ca++, Mg++ and Na+ on Heat Aggregation of Whey Protein ConcentratesJournal of Food Science, 1983
- Preferential interactions of proteins with salts in concentrated solutionsBiochemistry, 1982
- The Influence of Processing Parameters on Food Protein Functionality I. Differential Scanning Calorimetry as an Indicator of Protein DenaturationCanadian Institute of Food Science and Technology Journal, 1981
- Multiple regression and response surface analysis of the effects of calcium chloride and cysteine on heat-induced whey protein gelationJournal of Agricultural and Food Chemistry, 1979
- Salt effects on hydrophobic interactions in precipitation and chromatography of proteins: An interpretation of the lyotropic seriesArchives of Biochemistry and Biophysics, 1977