1970•Journal of Dairy ResearchRequires access

The denaturation of α-lactalbumin and β-lactoglobulin in heated milk

R. L. J. Lyster

Open publisher page 167 citations

Abstract

Summary The rates of denaturation by heat of α-lactalbumin and β-lactoglobulin in skim-milk were measured by an immunodiffusion method over a wide range of temperatures. Both reactions showed an unusual temperature dependence. The denaturation of α-lactalbumin is a first-order reaction; between 90 and 155 °C the kinetic constant k1in s−1is given by the equation whereTis the temperature in °K. The denaturation of β-actoglobulin in skim-milk is second order with respect to time, and the kinetic constant k2in 1g–1s–1is given by 2 equations, valid for different temperature ranges. Between 68 and 90 °C, Between 90 and 135 °C Results obtained by the immunodiffusion method agreed well with those found by salt fractionation of the milk proteins. The denaturation rates decreased when a specific reagent for sulphydryl groups was added, suggesting that such groups are involved in the denaturation of both proteins.

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Summary The rates of denaturation by heat of α-lactalbumin and β-lactoglobulin in skim-milk were measured by an immunodiffusion method over a wide range of temperatures. Both reactions showed an unusual temperature dependence. The denaturation of α-lactalbumin is a first-order reaction; between 90 and 155 °C the kinetic constant k1in s−1is given by the equation whereTis the temperature in °K. The denaturation of β-actoglobulin in skim-milk is second order with respect to time, and the kinetic constant k2in 1g–1s–1is given by 2 equations, valid for different temperature ranges. Between 68 and 90 °C, Between 90 and 135 °C Results obtained by the immunodiffusion method agreed well with those found by salt fractionation of the milk proteins. The denaturation rates decreased when a specific reagent for sulphydryl groups was added, suggesting that such groups are involved in the denaturation of both proteins.

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Available abstract

Summary The rates of denaturation by heat of α-lactalbumin and β-lactoglobulin in skim-milk were measured by an immunodiffusion method over a wide range of temperatures. Both reactions showed an unusual temperature dependence. The denaturation of α-lactalbumin is a first-order reaction; between 90 and 155 °C the kinetic constant k1in s−1is given by the equation whereTis the temperature in °K. The denaturation of β-actoglobulin in skim-milk is second order with respect to time, and the kinetic constant k2in 1g–1s–1is given by 2 equations, valid for different temperature ranges. Between 68 and 90 °C, Between 90 and 135 °C Results obtained by the immunodiffusion method agreed well with those found by salt fractionation of the milk proteins. The denaturation rates decreased when a specific reagent for sulphydryl groups was added, suggesting that such groups are involved in the denaturation of both proteins.

Key concepts: Denaturation (fissile materials), Chemistry, Skimmed milk, Lactalbumin, Chromatography, Reagent, Radial immunodiffusion, Physical chemistry

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