RESUMO
We used computational molecular dynamics (MD) to assess molecular conformations of apo- and holo-forms (respectively without and with Ca2+) of bovine α-lactalbumin (α-La) at different temperatures, and to correlate them with the protein's foaming properties. At 4 °C and 25 °C no major protein conformation changes occurred. At 75 °C, lots of changes were evidenced: the Ca2+ depletion triggered the complete loss of h2b, h3c helices and S1, S2 and S3 ß-sheets, and partial losses of H1, H2 and H3 α-helices. The absence of Ca2+ in apo-α-La and its leaving from holo-α-La triggered electrostatic repulsion among Asp82, Asp84 and Asp87, leading to the formation of a hydrophobic cluster involving Phe9, Phe31, Ile1, Va42, Ile55, Phe80 and Leu81. These conformational changes were related to an interfacial tension decrease and to a foaming capacity increase, for both apo-α-La and holo-α-La. This study exemplifies how powerful MD is as a tool to provide a better understanding of the molecular origins of food proteins' techno-functionalities.
