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

IF 3.7 Q2 CHEMISTRY, PHYSICAL

ACS Physical Chemistry Au Pub Date : 2024-09-12 DOI:10.1021/acsphyschemau.4c00029

Judith Peters, Karin Kornmueller, Rim Dannaoui, Ejona Syla, Annalisa Pastore

引用次数: 0

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.

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用差示扫描量热法直接检测溶菌酶水合粉末中的结合水

在通过差示扫描量热法研究溶菌酶粉末在不同复水百分比下的行为时，我们注意到在散装水熔点的左侧持续存在一个小峰值，当加热系统时，该峰值始终在-10 °C左右。该转变的强度在复水 160% 时达到最大，在更高值时消失。通过比较 H2O 和 D2O 中预熔峰的特性，我们将其归因于结合在蛋白质表面的可冻结水。这是首次报道这种观察结果。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

ACS Physical Chemistry Au 物理化学-

CiteScore

3.70

自引率

0.00%

发文量

期刊介绍： ACS Physical Chemistry Au is an open access journal which publishes original fundamental and applied research on all aspects of physical chemistry. The journal publishes new and original experimental computational and theoretical research of interest to physical chemists biophysical chemists chemical physicists physicists material scientists and engineers. An essential criterion for acceptance is that the manuscript provides new physical insight or develops new tools and methods of general interest. Some major topical areas include:Molecules Clusters and Aerosols; Biophysics Biomaterials Liquids and Soft Matter; Energy Materials and Catalysis