Effect of Heat Treatment on Denaturation of Bovine α-Lactalbumin:  Determination of Kinetic and Thermodynamic Parameters

Zeina Wehbi, María-Dolores Pérez,* Lourdes Sánchez, Coloma Pocoví, Chokry Barbana, and Miguel Calvo
Tecnologa y Bioqumica de los Alimentos, Facultad de Veterinaria, Universidad de Zaragoza, c/Miguel Servet 177, 50013 Zaragoza, Spain
J. Agric. Food Chem., 2005, 53 (25), pp 9730–9736
DOI: 10.1021/jf050825y
Publication Date (Web): November 11, 2005
Copyright © 2005 American Chemical Society
*

 Author to whom correspondence should be addressed (telephone 34 976 761585; fax 34 976 761612; e-mail dperez@unizar.es).

Abstract

The effect of heat treatment on the denaturation of α-lactalbumin was studied, under different conditions, over a temperature range of 78−94 °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 α-lactalbumin, measured by the loss of immunoreactivity, could be described as an order of reaction of n = 1.5. Results obtained indicated that α-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-α-lactalbumin decreased with the binding of oleic acid.

Keywords: Heat denaturation; bovine milk; native lactalbumin; apo-α-lactalbumin; kinetics; thermodynamics

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History

  • Published In Issue December 14, 2005
  • Received for review April 12, 2005. Revised manuscript received September 16, 2005. Accepted September 28, 2005. This work was supported by Grants ALI97-1041 and AGL2001-1814 from CICYT.

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