Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 53, Issue 25, Pages 9730-9736Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf050825y
Keywords
heat denaturation; bovine milk; native lactalbumin; apo-alpha-lactalbumin; kinetics; thermodynamics
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The effect of heat treatment on the denaturation of (x-lactalbumin was studied, under different conditions, over a temperature range of 78-94 degrees C. The concentration of the residual immunoreactive protein after different treatments was determined by kinetic analysis, obtaining D and Z values. Thermodynamic parameters were also calculated. Denaturation of alpha-lactalbumin, measured by the loss of immunoreactivity, could be described as an order of reaction of n = 1.5. Results obtained indicated that a-lactalbumin was more heat-sensitive when treated in milk than in phosphate buffer. The protein was also denatured more rapidly in the apo form than in the calcium-saturated form. Besides, the thermal stability of apo-alpha-lactalbumin decreased with the binding of oleic acid.
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