Use of differential scanning calorimetry and infrared spectroscopy in the study of thermal and structural stability of alpha-lactalbumin

被引：65

作者：

Boye, JI ^{[1
]}

Alli, I ^{[1
]}

Ismail, AA ^{[1
]}

机构：

[1] MCGILL UNIV, DEPT FOOD SCI & AGR CHEM, MONTREAL, PQ H9X 3V9, CANADA

来源：

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY | 1997年 / 45卷 / 04期

关键词：

alpha-lactalbumin; infrared spectroscopy; differential scanning calorimetry; denaturation; secondary structure;

D O I：

10.1021/jf960360z

中图分类号：

S [农业科学];

学科分类号：

09 ;

摘要：

Structural changes of alpha-lactalbumin (alpha-lac) in response to pH, ionic strength, sugars, and heat treatment were investigated by differential scanning calorimetry (DSC) and Fourier transform infrared (FTIR) spectroscopy. From DSC, two reversible transitions at 39.6 degrees C (A) and 64.8 degrees C (B) were observed when alpha-lac was heated. At pH 3, transition A was partially reversible (14%) while transition B was completely reversible. At pH 9, both transitions were completely irreversible. Heating alpha-lac at pH 3 resulted in aggregation with no observed gelation; at pH 9 a translucent gel was formed. FTIR showed that at pH 3, denaturation of alpha-lac resulted in the appearance of two bands at 1616 and 1685 cm(-1) attributed to intermolecular aggregation. These bands were absent at alkaline pH. The major effects of heat treatment of alpha-lac were loss in the bands attributed to alpha-helix, 3(10)-helix, and beta-sheet and increase in the bands attributed to turns.

引用

页码：1116 / 1125

页数：10

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