Direct Detection of Bound Water in Hydrated Powders of Lysozyme by Differential Scanning Calorimetry

ACS Phys Chem Au. 2024 Sep 12;4(6):593-597. doi: 10.1021/acsphyschemau.4c00029. eCollection 2024 Nov 27.

Abstract

While exploring the behavior of lysozyme powders at different percentages of rehydration by differential scanning calorimetry, we noticed a small peak persistently on the left of the melting point of bulk water, which, when heating up the system, was always around -10 °C. The intensity of the transition was maximal at 160% rehydration and disappeared at higher values. By comparing the premelting peak properties in H2O and D2O, we attributed it to freezable water bound on the protein surface. This is the first time that such an observation has been reported.