NDLI: Glass Transition and Dynamics in Lysozyme–Water Mixtures Over Wide Ranges of Composition

Content Provider	Springer Nature Link
Author	Panagopoulou, Anna Kyritsis, Apostolos Aravantiu, Anna Maria Napoulos, Dionysios i Serra, Roser Sabater Gómez Ribelles, Jose Luis Shinyashiki, Naoki Pissis, Polycarpos
Copyright Year	2011
Abstract	Differential scanning calorimetry (DSC) and two dielectric techniques, broadband dielectric relaxation spectroscopy and thermally stimulated depolarization currents (TSDC), were employed to study glass transition and water and protein dynamics in mixtures of water and a globular protein, lysozyme, in wide ranges of water content, both solutions, and hydrated solid samples. In addition, water equilibrium sorption isotherms (ESI) measurements were performed at room temperature. The main objective was to correlate results by different techniques to each other and to determine critical water contents for various processes. From ESI measurements the content of water directly bound to primary hydration sites was determined to 0.088 (grams of water per grams of dry protein), corresponding to 71 water molecules per protein molecule, and that where clustering becomes significant to about 0.25. Crystallization and melting events of water were first observed at water contents 0.270 and 0.218, respectively, and the amount of uncrystallized water was found to increase with increasing water content. Two populations of ice crystals were observed by DSC, primary and bulk ice crystals, which give rise to two separate relaxations in dielectric measurements. In addition, the relaxation of uncrystallized water was observed, superimposed on a local relaxation of polar groups on the protein surface. The glass transition temperature, determined by DSC and TSDC in rather good agreement to each other, was found to decrease significantly with increasing water content and to stabilize at about −90 °C for water contents higher than about 0.25. This is a novel result of this study with potential impact on cryoprotection and pharmaceutics.
Starting Page	199
Ending Page	209
Page Count	11
File Format	PDF
ISSN	15571858
Journal	Food Biophysics
Volume Number	6
Issue Number	2
e-ISSN	15571866
Language	English
Publisher	Springer US
Publisher Date	2011-01-13
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Glass transition Molecular mobility Hydrated proteins Uncrystallized water Dielectric relaxation Plasticization Analytical Chemistry Food Science Biophysics and Biological Physics
Content Type	Text
Resource Type	Article
Subject	Analytical Chemistry Biophysics Bioengineering Food Science Applied Microbiology and Biotechnology

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