Masters Theses
Abstract
"The phase reversal of an emulsion from a system in which oil droplets are dispersed in a water medium to a system in which water droplets are dispersed in oil is dependent upon the interfacial characteristics of the liquids and the emulsifying agent being used, as well as the volume ratio of the two liquid phases. A preliminary investigation at this institution has indicated a possible relationship between phase reversal and the isoelectric point of gelatin used as the emulsifying agent. Since the properties of proteins vary so greatly with the hydrogen ion concentration, particularly near their isoelectric points, research into emulsion phase reversals with varying pH could give an insight into the mechanism of emulsion formation and behavior.
Liquids chosen for the immiscible oil phase were organic substances for which phase reversals have been reported. They included both cyclic and long and short straight-chain hydrocarbons representing wide ranges in viscosity, density, and surface tension.
The proteins chosen as emulsifying agents varied greatly in their structure. The simple proteins used were zein, a prolamine, and gelatin, a mixture of hydrolyzed albuminoids. The class of conjugated proteins was represented by the phosphoprotein, casein"--Introduction, pages 1-2.
Advisor(s)
Fisher, Emory D.
Department(s)
Chemistry
Degree Name
M.S. in Chemistry
Publisher
Missouri School of Mines and Metallurgy
Publication Date
1956
Pagination
vi, 57 pages
Note about bibliography
Includes bibliographical references (pages 53-56).
Rights
© 1956 Samuel Arthur Bradford, All rights reserved.
Document Type
Thesis - Open Access
File Type
text
Language
English
Subject Headings
EmulsionsProteinsHydrogen-ion concentration
Thesis Number
T 1125
Print OCLC #
5920258
Electronic OCLC #
945211658
Recommended Citation
Bradford, Samuel Arthur, "The effect of pH on phase reversals of protein-stabilized emulsions" (1956). Masters Theses. 2575.
https://scholarsmine.mst.edu/masters_theses/2575