Modification of Egg White Proteins with Oleic Acid

Abstract

Studies on the chemical modification of egg white with oleic acid (5-50 moles/50,000g of egg white protein) revealed that the reagent partitioned equally between supernatant and precipitate. The mole ratio of oleic acid to protein in solution at the 20 mole level of treatment was 14.6:1. Oleic acid did not selectively precipitate ovalbumin, conalbumin, or lysozyme. An increase in negative charge of proteins was observed in the chromatograms of treated egg white. No difference in molecular weights of treated egg white proteins was observed. The viscosity varied with the concentration of the reagent. In cooked, frozen, and thawed egg white water retaining index was 1.5-10X greater for treated than untreated material.

Effect of different concentrations of olive oil and oleic acid on the mechanical properties of albumen (egg white) edible films

“…However, oleic acid did not affect (P < 0.05) the WVP of albumin films in our study. King et al (1984) observed an increase of negative charge in albumin proteins treated with oleic acid. Oleic acid likely increased negative charges (and hydrophilicity) along albumin protein chains, thus negating the hydrophobic effect of fatty acid acyl chains.…”

“…As mentioned, oleic acid introduced negative charges (carboxyl groups) to albumin proteins (King et al, 1984;Ball, 1987). The improve texture and increasing film tensile strength is due to poor structural properties integrity; different lipids also have reduced extensibility of protein films.…”

Thermally Induced Gelation of Native and Modified Egg White‐Rheological Changes During Processing; Final Strengths and Microstructures

“…Succinylation was performed by the method of Ball and Winn (1982) by the addition of 15 moles reagent/50000g protein. Treatment with oleic acid was performed as described by King et al (1984) to a level of 15 moles reagent/50000g protein. The final pH for native and modified egg white was adiusted to 9.0 by the addition of 1N NaOH.…”

“…Egg white is widely used in the food industry because of its important functional properties. Chemical modification of egg white proteins has been carried out by several researchers to improve their biophysical and functional properties (Gandhi et al, 1968a,b;Sato and Nakamura, 1977;Ball and Winn, 1982;King et al, 1984) or to help in the study of protein gelation (Shimada and Matsushita, 1980;Ma and Holme, 1982). In a previous study (Montejano et al, 1984a) the mechanical failure characteristics of heat-induced gels from native egg white and egg white modified with acetic anhydride, succinic anhydride or oleic acid were evaluated.…”

Preventive Effect of Egg Yolk Phosvitin on Heat-Insolubilization of Egg White Protein and Its Application to Heat-Induced Egg White Gel

“…[1][2][3] Therefore, the pasteurization of egg white to prevent insolubilization is carried out for a few minutes at a temperature near 60 C. On the other hand, in order to stabilize EWP against heat aggregation and potential precipitation, the effects of treatments with acylating reagents, 4,5) fatty acids, 6) anionic detergents, 7) and polyols 8) have been investigated. King et al 9) reported that an increase in negative charge of EWP by adding oleic acid or sodium dodecyl sulfate (SDS) altered thermal denaturation and improved the properties of EWP gel. We showed in a previous paper that dextran sulfate suppresses the heat-insolubilization of EWP, and that a transparent, firm gel can be prepared from EWP by the addition of dextran sulfate, an anionic polysaccharide, on heating.…”