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Lysozyme-water interactions studied by sorption calorimetry

Kocherbitov, Vitaly LU ; Arnebrant, T and Söderman, Olle LU (2004) In The Journal of Physical Chemistry Part B 108(49). p.19036-19042
Abstract
Hydration of hen egg white lysozyme was studied by using the method of sorption calorimetry at 25, 40, and 50degreesC. Desorption calorimetric measurements were performed at 25 and 40degreesC. The activity of water and partial molar enthalpy of mixing of water were determined as functions of water content. Hydration of lysozyme occurs in four steps: slow penetration of water into the protein-protein interface; gradual glass transition, which occurs in every protein molecule independently of other molecules; further water uptake with disaggregation of protein aggregates and formation of a monolayer of water; and accumulation of free water. The amount of bound water found in desorption experiments is 420 water molecules per lysozyme... (More)
Hydration of hen egg white lysozyme was studied by using the method of sorption calorimetry at 25, 40, and 50degreesC. Desorption calorimetric measurements were performed at 25 and 40degreesC. The activity of water and partial molar enthalpy of mixing of water were determined as functions of water content. Hydration of lysozyme occurs in four steps: slow penetration of water into the protein-protein interface; gradual glass transition, which occurs in every protein molecule independently of other molecules; further water uptake with disaggregation of protein aggregates and formation of a monolayer of water; and accumulation of free water. The amount of bound water found in desorption experiments is 420 water molecules per lysozyme molecule. Two hysteresis loops were found in the sorption isotherm of lysozyme. The small loop is caused by the slow penetration of water molecules into the protein-protein interface at very low water contents, while the large loop is due to the slow kinetics of aggregation of protein molecules upon desorption. The phase diagram of the lysozyme-water system is presented. (Less)
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
The Journal of Physical Chemistry Part B
volume
108
issue
49
pages
19036 - 19042
publisher
The American Chemical Society
external identifiers
  • wos:000225548700037
  • scopus:10844239741
ISSN
1520-5207
DOI
10.1021/jp0476388
language
English
LU publication?
yes
id
cb437336-fd0c-487a-a4f8-49c365159bc3 (old id 153961)
date added to LUP
2007-07-11 14:44:31
date last changed
2017-09-03 04:37:12
@article{cb437336-fd0c-487a-a4f8-49c365159bc3,
  abstract     = {Hydration of hen egg white lysozyme was studied by using the method of sorption calorimetry at 25, 40, and 50degreesC. Desorption calorimetric measurements were performed at 25 and 40degreesC. The activity of water and partial molar enthalpy of mixing of water were determined as functions of water content. Hydration of lysozyme occurs in four steps: slow penetration of water into the protein-protein interface; gradual glass transition, which occurs in every protein molecule independently of other molecules; further water uptake with disaggregation of protein aggregates and formation of a monolayer of water; and accumulation of free water. The amount of bound water found in desorption experiments is 420 water molecules per lysozyme molecule. Two hysteresis loops were found in the sorption isotherm of lysozyme. The small loop is caused by the slow penetration of water molecules into the protein-protein interface at very low water contents, while the large loop is due to the slow kinetics of aggregation of protein molecules upon desorption. The phase diagram of the lysozyme-water system is presented.},
  author       = {Kocherbitov, Vitaly and Arnebrant, T and Söderman, Olle},
  issn         = {1520-5207},
  language     = {eng},
  number       = {49},
  pages        = {19036--19042},
  publisher    = {The American Chemical Society},
  series       = {The Journal of Physical Chemistry Part B},
  title        = {Lysozyme-water interactions studied by sorption calorimetry},
  url          = {http://dx.doi.org/10.1021/jp0476388},
  volume       = {108},
  year         = {2004},
}