Solvent-induced lysozyme gels:: Effects of system composition and temperature on structural and dynamic characteristics

被引：16
作者：
da Silva, Marcelo A.
Farhat, Imad A.
Areas, Elizabeth P. G.
Mitchell, John R.
机构：
[1] Univ Sao Paulo, Inst Quim, Dept Quim Fundamental, BR-05513970 Sao Paulo, SP, Brazil
[2] Univ Nottingham, Sch Biosci, Div Food Sci, Loughborough LE12 5RD, Leics, England
来源：
BIOPOLYMERS | 2006年 / 83卷 / 05期
关键词：
sol-gel processes; globular protein; rheology; infrared spectroscopy; differential scanning calorimetry;
D O I：
10.1002/bip.20561
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The gelation process of lysozyme in water/tetramethylurea in the presence of salt was investigated as a function of temperature and system composition by rheology, infrared spectroscopy, and microcalorimetry. Times and temperatures of gelation were determined from the variation of the storage (G') and loss (G") moduli. It was found that gelation times follow exponential decays with both protein and tetramethylurea (TMU) concentrations and with temperature. The activation energy for the overall process shows a linear dependence on TMU mass fraction. A strongly increased beta-sheet content and reduced a-helix occur with the increase of TMU concentration in the binary solvent. Also, a linear decrease of lysozyme denaturation temperature and enthalpy on TMU concentration is found for the TMU mass fraction up to 0.5, above which no denaturation signal can be detected. (c) 2006 Wiley Periodicals, Inc.
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收藏
页码：443 / 454
页数：12
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