Stabilizers of horseradish peroxidase.
- Author:
Xinhuan MAO
1
;
Xiang LI
;
Shanshan WANG
;
Wenjing ZHANG
;
Chengming ZENG
Author Information
1. College of Chemistry and Material Sciences, Shaanxi Normal University, Xi'an 710062, China.
- Publication Type:Journal Article
- MeSH:
Drug Synergism;
Enzyme Stability;
drug effects;
Gelatin;
pharmacology;
Horseradish Peroxidase;
metabolism;
Hot Temperature;
Magnesium Sulfate;
pharmacology
- From:
Chinese Journal of Biotechnology
2009;25(3):388-391
- CountryChina
- Language:Chinese
-
Abstract:
Keeping an enzyme in its native form with high catalytic activity is of great significance. In the present study, thermal stabilizers of horseradish peroxidase (HRP) were screened. The results indicated that thermal stability of HRP was enhanced by magnesium sulphate and gelatin. A synergic effect of magnesium sulphate and gelatin was observed. In the presence of the stabilizer, the enzymatic activity of HRP remained 89% after kept for 80 h at 50 degrees C and 57% for 90 days at room temperature. Thermal alterations of HRP structure in the absence and presence of the stabilizers were explored by using UV absorption spectra at 402 nm (Soret band), intrinsic fluorescence and 8-anilinonaphthalene-1-sulfonic acid (ANS) fluorescence. The results suggested that magnesium sulphate and gelatin attenuated the extent of unfolding of HRP and therefore the native enzyme structure was stabilized.
