NMR and DSC studies during thermal denaturation of collagen

被引：76

作者：

Rochdi, A ^{[1
]}

Foucat, L ^{[1
]}

Renou, JP ^{[1
]}

机构：

[1] INRA, Rech Viande Stn, Struct Tissulaires & Interact Mol, F-63122 St Genes Champanelle, France

来源：

FOOD CHEMISTRY | 2000年 / 69卷 / 03期

关键词：

collagen; thermal denaturation; NMR; DSC;

D O I：

10.1016/S0308-8146(99)00267-8

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

Epimysial and intramuscular connective tissues from calf and cow muscle were 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 temperature and the variation enthalpy of sol-->gel transition. According to the heating time, significant differences were observed between tissues. NMR discriminated the type of collagen whereas DSC distinguished the age of tissue. Differences were related to the degree of protein hydration, emphasising the complementary information from these two analytical tools. (C) 2000 Elsevier Science Ltd. Ail rights reserved.

引用

页码：295 / 299

页数：5

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