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

被引：0
|
作者：
Peters, Judith [1 ,2 ,3 ]
Kornmueller, Karin [4 ]
Dannaoui, Rim [1 ,2 ]
Syla, Ejona [1 ,2 ]
Pastore, Annalisa [1 ]
机构：
[1] Universite Grenoble Alpes, CNRS, LIPhy, F-38000 Grenoble, France
[2] Inst Laue Langevin, F-38042 Grenoble, France
[3] Inst Univ France, F-75231 Paris, France
[4] Med Univ Graz, Gottfried Schatz Res Ctr Cell Signaling, Metab & Aging Biophys Div, A-8010 Graz, Austria
来源：
ACS PHYSICAL CHEMISTRY AU | 2024年 / 4卷 / 06期
关键词：
bound and bulk water; hydrated protein powders; liquid-to-solid transition; protein stability; DSC measurements; COLD DENATURATION; PROTEIN; TEMPERATURE; PRESSURE; H2O;
D O I：
10.1021/acsphyschemau.4c00029
中图分类号：
O64 [物理化学（理论化学）、化学物理学];
学科分类号：
070304 ; 081704 ;
摘要：
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 degrees 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.
引用
收藏
页码：593 / 597
页数：5
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