Probing the structure-holding interactions in cheeses by dissociating agents: a review and an experimental evaluation with emmental cheese

Interactions holding protein structure in cheese has been a subject of considerable investigation, with conclusions varying among studies. We present a review on this topic, covering fresh curds, ripened cheeses, and processed cheeses. We discuss the usual chemicals and conditions used to probe different types of interactions. Furthermore, we did our own study with solutions of urea, SDS, EDTA, NaCl, and NaOH, at different concentrations and combinations, for Emmental cheese. To quantify solubilized protein, we developed a modification of a spectrometric-based method that can be conveniently employed to quantify total protein in cheese, with statistically similar results to those obtained by the Kjeldahl method. Our results point out that caseins in the Emmental cheese are held together by a set of hydrophobic interactions, hydrogen bonds, and other electrostatic ones, including ionic bonds. Hydrogen bonds seem to have an important role, comparable to hydrophobic interactions, a conclusion not commonly reported for cheese structures.