Amylose-lipid complex dissociation. A study of the kinetic parameters

Abstract

The kinetic parameters for the dissociation of the amylose-1-α-lysophosphatidilcholine complex were studied by differential scanning calorimetry, using the Borchardt–Daniels and dynamic methods. The reaction order was found to be close to 1 with an activation energy of 419 kJ/mol and the results were verified by an isothermal method; it was found that the activation energy increases for increasing water content. Two endotherms were obtained in the isothermal experiments, suggesting the presence of two forms of the complex, one more kinetically stable than the other. © 1999 John Wiley & Sons, Inc. Biopoly 49: 81–89, 1999