Interaction entre un peptide de β-lactoglobuline bovine (β-lg f1-8) et les protéines du lactosérum : le cas de l’a-lactalbumine
|Advisor:||Pouliot, Yves; Gauthier, Sylvie|
|Abstract:||Preliminary observations showed that the self-assembly capacity of a β-lactoglobulin peptide obtained from trypsin hydrolysis (β-lg f1-8) could modify the composition of whey protein mixtures, mainly by reducing the amount of soluble α-lactalbumin (α-la). The goal of this study was to demonstrate the occurrence of interactions between β-lg f1-8 peptide and α-la. A study of the peptide self-assembly process in presence of α-la at 25 and 55 °C showed that the addition of α-la to the original tryptic hydrolysate delays the flocculation of peptide β-lg f1-8 at 55 °C. Adding β-lg f1-8 peptide to α-la modified the solubility profile of the protein at various pH, but its thermal unfolding profile obtained by differential scanning calorimetry (DSC) remained unchanged. All of these observations suggest that the peptide β-lg f1-8 can interact with the α-la via hydrophobic interactions and could be used for developing new strategies for the fractionation of protein mixtures.|
|Document Type:||Mémoire de maîtrise|
|Open Access Date:||19 April 2018|
|Collection:||Thèses et mémoires|
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