Inactivation kinetics of horseradish peroxidase in organic solvents of different hydrophobicity at different water contents

被引:6
|
作者
Saraiva, J
Oliveira, JC
Oliveira, S
Hendrickx, M
机构
[1] UNIV CATOLICA PORTUGUESA, ESCOLA SUPER BIOTECNOL, P-4200 Porto, PORTUGAL
[2] KATHOLIEKE UNIV LEUVEN, FAC AGR & APPL BIOL SCI,CTR FOOD SCI & TECHNOL, B-3001 HEVERLEE, BELGIUM
关键词
biocatalysis; enzyme thermal inactivation; time-temperature integrators; water activity;
D O I
10.1046/j.1365-2621.1996.00343.x
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
The thermal stability of horseradish peroxidase suspensions was studied in three organic solvents of different hydrophobicity (dodecane, octane, and I-octanol) at three different water contents (14.1, 55.3 and 256.2 mg water g(-1) dry protein). In these conditions, the enzyme is much more stable than in aqueous solutions (inactivation temperatures were in the range of 125-150 degrees C). The enzyme showed a similar stability when in the presence of organic solvents, compared to the enzyme in a solid matrix without organic solvents with the same water content. The inactivation kinetics was well described by assuming the existence of two iso-enzymes, both inactivating according to a first order model. The lowest value for the z-value of both fractions (around 15 degrees C) was obtained at the higher water content studied. The use of solvent and water content variables should be adequate to develop time-temperature integrators to monitor thermal processes at 100-140 degrees C.
引用
收藏
页码:233 / 240
页数:8
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