Kinetics of thermal inactivation of catalase in the presence of additives

被引：12

作者：

Cantemir, Anca Ruxandra ^{[1
]}

Raducan, Adina ^{[1
]}

Puiu, Mihaela ^{[2
]}

Oancea, Dumitru ^{[1
]}

机构：

[1] Univ Bucharest, Fac Chem, Dept Phys Chem, Bucharest 030018, Romania

[2] Univ Bucharest, LaborQ, Bucharest 030018, Romania

来源：

PROCESS BIOCHEMISTRY | 2013年 / 48卷 / 03期

关键词：

Catalase; Hydrogen peroxide decomposition; Kinetics of thermal inactivation; STABILIZATION; PARAMETERS; THERMOSTABILITY; AGGREGATION; STABILITY; MECHANISM; GLUCOSE; ENZYMES;

D O I：

10.1016/j.procbio.2013.02.013

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The kinetics of catalase inactivation in buffer-free aqueous solutions within the temperature range 30-60 degrees C in the absence or presence of hydrogen peroxide was investigated and discussed taking into account the effect of NaCl, ethane-1,2-diol, propane-1,2,3-triol and sucrose, additives expected to increase the enzyme thermostability. Using the kinetic extended curves obtained by measuring the substrate absorbance in time and an isoconversional method, several simple kinetic models most frequently encountered in literature were fitted to the experimental data. The best model for inactivation was chosen on the basis of several statistical criteria. The half-times of inactivation and the activation energies were also reported and discussed. (C) 2013 Elsevier Ltd. All rights reserved.

引用

页码：471 / 477

页数：7

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