title: Analysis of the thermally induced structural changes of bovine lactoferrin.
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.
authors: Faculty of Food Science and Engineering, "Dunarea de Jos" University of Galati , 111 Domneasca Street, 800201, Galati, Romania.
authors: Nicoleta
authors: N
authors: Stănciuc
authors: Iuliana
authors: I
authors: Aprodu
authors: Gabriela
authors: G
authors: Râpeanu
authors: Iesel
authors: I
authors: van der Plancken
authors: Gabriela
authors: G
authors: Bahrim
authors: Marc
authors: M
authors: Hendrickx
mesh_terms: D000818:Animals; D002417:Cattle; D006358:Hot Temperature; D006868:Hydrolysis; D057927:Hydrophobic and Hydrophilic Interactions; D007781:Lactoferrin / Q000737:chemistry* / Q000302:isolation & purification; D008958:Models, Molecular; D011487:Protein Conformation; D012996:Solutions; D013050:Spectrometry, Fluorescence; D013820:Thermolysin / Q000378:metabolism
chemical_list: D012996:Solutions; D007781:Lactoferrin; D013820:Thermolysin