Rheological characteristics of β-lipoproteins

The apparent viscosity of β‐lactoglobulin solutions was studied as a function of shear rate using a cone and plate uiscometer (Ferranti‐Shirley Viscometer System). Aqueous buffered solutions (pH 7, ionic strength 0.04) containing up to 40% protein were subjected to a rate of shear between 800 and 17,000 sec ‐1. At protein concentrations of 5% and lower, the viscosity was independent of the shear rate or the time of shearing. At protein concentrations of 10% or higher, the viscosity decreased asymptotically with an increasing shear rate. At a constant shear rate, the viscosity of 10‐30%β‐lactoglobulin solutions increased with shearing time. However, this rheopectic property was not consistently observed but, rather, was dependent on the rate of shear at concentrations lower than 20%. A rheopectic hysteresis effect was observed for 10‐30% protein solutions whereas thixotropy was observed for 40% solutions. The rheopectic nature appeared to be the result of the permanent denaturation of protein characterized by UV absorption and gel filtration.

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“…1973; Mancuso e t al. 1973;Silvestro 1973;Libondi et al 1974;Maruyama et al 1974;Puri and Bala 1975;Dokic and Kjakovic 1975).…”

Section: Introductionmentioning

confidence: 99%

PSEUDOPLASTIC AND RHEOPECTIC PROPERTIES OF A GLOBULAR PROTEIN (β‐LACTOGLOBULIN) SOLUTION¹

Pradipasena

Rha

1977

Journal of Texture Studies

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Milk proteins: Physicochemical and functional properties

1984

C R C Critical Reviews in Food Science and Nutrition

551

294

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Because of the growing trend toward widespread use of protein ingredients in food formulation and fabrication, an understanding of the relationships between the physical properties of proteins and their behavior in food systems is desirable. A range of milk-derived protein preparations, i.e., dry milk, milk proteins, caseins, whey proteins, and lactalbumin, are used in a range of food products for their specific functional attributes. In this paper some of the apparent relationships between the properties of the protein components and specific functional properties are discussed. Thus, the roles of milk proteins in determining some important physical characteristics (i.e. color, bulk density, sinkability, dispersibility) of milk powders and their involvement in a range of functional properties (water holding, solubility, rheological behavior, gelation, film formation, emulsification, and foaming) are reviewed. Because of the various methods and conditions used in determining functional properties and the variability in composition of preparations it is difficult to compare data and/or reconcile differences in published information. The desirability of developing standard methods is emphasized.

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Eine rheologische Studie an Plasma-Lipoproteinen

Schurz¹,

Alloush²,

Farhoudi³

et al. 1977

Hoppe-Seyler´s Zeitschrift für physiologische Chemie

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Rheological characteristics of β-lipoproteins

Cited by 3 publications

References 12 publications

PSEUDOPLASTIC AND RHEOPECTIC PROPERTIES OF A GLOBULAR PROTEIN (β‐LACTOGLOBULIN) SOLUTION¹

PSEUDOPLASTIC AND RHEOPECTIC PROPERTIES OF A GLOBULAR PROTEIN (β‐LACTOGLOBULIN) SOLUTION¹

Milk proteins: Physicochemical and functional properties

Eine rheologische Studie an Plasma-Lipoproteinen

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Rheological characteristics of β-lipoproteins

Cited by 3 publications

References 12 publications

PSEUDOPLASTIC AND RHEOPECTIC PROPERTIES OF A GLOBULAR PROTEIN (β‐LACTOGLOBULIN) SOLUTION1

PSEUDOPLASTIC AND RHEOPECTIC PROPERTIES OF A GLOBULAR PROTEIN (β‐LACTOGLOBULIN) SOLUTION1

Milk proteins: Physicochemical and functional properties

Eine rheologische Studie an Plasma-Lipoproteinen

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Product

Resources

About

PSEUDOPLASTIC AND RHEOPECTIC PROPERTIES OF A GLOBULAR PROTEIN (β‐LACTOGLOBULIN) SOLUTION¹

PSEUDOPLASTIC AND RHEOPECTIC PROPERTIES OF A GLOBULAR PROTEIN (β‐LACTOGLOBULIN) SOLUTION¹