The Protective Effect of Small Amounts of Anionic Detergents on the Thermal Aggregation of Crude Ovalbumin

Hegg, Per‐Olof; Löfqvist, Bo

doi:10.1111/j.1365-2621.1974.tb07362.x

Cited by 31 publications

(21 citation statements)

References 11 publications

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“…However, certain anionic detergents may also stabilize proteins against thermal aggregation. 200 Perutz's 341 recent discussion of the sequence of denaturation of hemoglobin is relevant. He suggested that denaturation by acid or alkali probably involves two effects, via the impact on total surface change of the protein and on the ionization of specific groups on particular amino acids.…”

Section: Denaturation and Functionalitymentioning

confidence: 98%

Functional properties of proteins in foods: A survey

Kinsella

Melachouris²

1976

C R C Critical Reviews in Food Science and Nutrition

1,202

677

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Section: Denaturation and Functionalitymentioning

confidence: 98%

Functional properties of proteins in foods: A survey

Kinsella

Melachouris²

1976

C R C Critical Reviews in Food Science and Nutrition

1,202

677

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“…Boyer et al (1946a, b) observed that low concentrations of fatty acids could stabilize bovine serum albumin against denaturation by heat, urea, or guanidine. Hegg and Lofquist (1974) reported that the aggregation temperature of crude ovalbumin was elevated in the presence of low concentrations of sodium dodecyl sulfate, 2-decylcitric acid, and lauric acid. These investigators proposed using fatty acids to obtain comparable results.…”

Section: Many Investigationsmentioning

confidence: 99%

Modification of Egg White Proteins with Oleic Acid

King¹,

Ball²,

Catignani³

et al. 1984

Journal of Food Science

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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.

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“…The difference in results between the no pH adjustment and pH 7 adjusted samples shows that pH of the testing dispersion has a very significant impact on protein's thermal stability. Hegg and L€ ofqvist (1974) determined that at pH between 3 and 10, ovalbumin would aggregate with the most extensive degree at pH 5.5.…”

Section: Effect Of 75 C Heating On Thermal Stability Of Modified Fewmentioning

confidence: 99%

“…The use of food ingredients or additives in combination with sonication for the protein has shown some promise. The addition of anionic additives such as 2-decylcitric acid, sodium dodecyl sulfate (SDS), and lauric acid has been shown to improve the thermal stability of ovalbumin in weak alkaline pH regions (Hegg & L€ ofqvist, 1974). The authors speculated that the hydrophobic core of the protein may be stabilized by the interaction of the hydrocarbon chain of the additive.…”

Section: Introductionmentioning

confidence: 99%