Effect of Trehalose on Thermal Stability of Bovine Serum Albumin

被引：3
|
作者：
Lavecchia, Roberto [1 ]
Zuorro, Antonio [1 ]
机构：
[1] Univ Roma La Sapienza, Dept Chem Engn, I-00184 Rome, Italy
来源：
CHEMISTRY LETTERS | 2010年 / 39卷 / 01期
关键词：
HUMAN HEMOGLOBIN; WATER; PROTEINS;
D O I：
10.1246/cl.2010.38
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Trehalose at 10-30% (w/w) greatly stabilized bovine serum albumin (BSA) against thermal denaturation. The highest stabilization was reached in 30% trehalose at 65 degrees C, when the protein's half life was increased from 72 to 335 min. A kinetic analysis based on the Lumry-Eyring mechanism of inactivation showed that BSA denaturation can be described by a first-order rate expression with an apparent activation energy ranging from 238.1 to 246.4 kJ mol(-1).
引用
收藏
页码：38 / 39
页数：2
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