Abstract
Bovine lactoferrin (LF) is subjected to thermal processing during isolation for commercial use and while preparing milk products intended for infant nutrition. The present study is focused on the heat-induced structural changes of LF in buffer solution. Fluorescence spectroscopy, molecular modeling, and enzymatic hydrolysis studies were combined to extensively characterize LF thermal behavior. The temperature-induced changes induced on LF conformation were analyzed through intrinsic and ANS fluorescence parameters (intensity, maximum position, and parameter A value), the phase diagram method, and quenching experiments using acrylamide and iodide. A higher exposure of hydrophobic residues was highlighted through the molecular modeling approach, with a decrease in α-helix content from 23.5% to 21.2% when increasing the temperature from 25 °C to 80 °C. The experimental results demonstrate a more flexible conformation of the protein at higher temperature, thus facilitating the enzymatic hydrolysis by thermolysin.
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