Analysis by Raman spectroscopy of the conformational structure of whey proteins constituting fouling deposits during the processing in a heat exchanger

Whey protein fouling deposits generated on the hot wall downstream a plate heat exchanger were analyzed by micro Raman spectroscopy (MRS) carried out in the 800–1800 cm−1 range. Deposits were formed using a model beta-lactoglobulin (BLG) fouling solution which was made using a whey protein isolate powder (89 wt.% in BLG) and a known amount of calcium. Thermal denaturation of the fouling solution was also analyzed by MRS as well as isolated BLG aggregates obtained by microfiltration of heated solutions. Specific Raman signatures of aggregates were identified, which were not detected in the Raman spectra of denatured (i.e. unfolded BLG molecule) solutions. MRS analyses at different depths of the deposit reveal a loss of α-helix structures, as observed in denatured BLG solutions, without the detection of aggregate signatures. For the range of calcium content investigated (from 97 to 160 mg l−1), no effect of calcium ions on the molecular conformation of BLG within the deposit was shown. Of great significance, results suggest that, for our set of operating conditions used, the mass distribution of the fouling deposit in a plate heat exchanger is primarily controlled by the distribution of the unfolded protein generated by the denaturation process.

► Micro Raman spectroscopy analysis of the molecular structure of beta-lactoglobulin.
► Raman signatures of native, denatured (unfolded) and aggregated beta-lactoglobulin.
► Whey protein deposits reveal a loss of α-helix structures.
► Beta-lactoglobulin state is not aggregated at the deposit – stainless steel interface.
► Calcium ion does not change the beta-lactoglobulin molecular conformation within deposit.