Abstract
The stabilizing effect of glycerol on type I collagens (C) from rat tail tendon (RTC), calf skin (CSC), human placenta (HPC), and sheep skin (SSC) at elevated temperature and in urea was investigated. The protein denaturation was followed by means of differential UV-spectroscopy. The denaturation temperatures (T(d)) increased proportionally to the concentration of glycerol in the reaction medium. Equations for the dependence of T(d) glycerol concentration were derived. The calculated thermodynamic characteristics do not change significantly with increasing glycerol concentration. It was observed that, in the presence of glycerol, the collagen molecule was stabilized, not only by heating, but also by the action of urea. Copyright (C) 1999 Elsevier Science Ltd.
Original language | English |
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Pages (from-to) | 483-487 |
Number of pages | 5 |
Journal | Food Chemistry |
Volume | 66 |
Issue number | 4 |
DOIs | |
State | Published - Sep 1999 |
Keywords
- Collagen
- Denaturation
- Different species
- Glycerol
- Stabilization
- Urea