NMR and DSC studies during thermal denaturation of collagen

Citation
A. Rochdi et al., NMR and DSC studies during thermal denaturation of collagen, FOOD CHEM, 69(3), 2000, pp. 295-299
Citations number
18
Categorie Soggetti
Food Science/Nutrition
Journal title
FOOD CHEMISTRY
ISSN journal
03088146 → ACNP
Volume
69
Issue
3
Year of publication
2000
Pages
295 - 299
Database
ISI
SICI code
0308-8146(200005)69:3<295:NADSDT>2.0.ZU;2-S
Abstract
Epimysial and intramuscular connective tissues from calf and cow muscle wer e studied by NMR and DSC. Water proton NMR transverse relaxation times (T-2 ) were measured at 10 degrees C for both native and thermally-denatured at 90 degrees C for 30-360 min. DSC measurements were used to determine the te mperature and the variation enthalpy of sol-->gel transition. According to the heating time, significant differences were observed between tissues. NM R discriminated the type of collagen whereas DSC distinguished the age of t issue. Differences were related to the degree of protein hydration, emphasi sing the complementary information from these two analytical tools. (C) 200 0 Elsevier Science Ltd. Ail rights reserved.