Biochemical characterization of Santalum album (Chandan) leaf peroxidase

被引：6

作者：

Kumar P. ^{[1
]}

Kamle M. ^{[1
]}

Singh J. ^{[2
]}

机构：

[1] Central Institute for Subtropical Horticulture

[2] Department of Biotechnology, Punjab University

来源：

Physiology and Molecular Biology of Plants | 2011年 / 17卷 / 2期

关键词：

Heat stability; Native-PAGE; Peroxidases; Precipitation; Purification; Santalum album;

D O I：

10.1007/s12298-011-0054-x

中图分类号：

学科分类号：

摘要：

The Santalum peroxidase was extracted from the leaves and precipitated with double volume of chilled acetone. The optimum percent relative activity for the Santalum peroxidase was observed at pH 5. 0 and 50 °C temperature. The Santalum peroxidase per cent relative activity was stimulated in the presence of phenolic compounds like ferrulic acid and caffeic acids; however, indole-3-acetic acid (IAA) and protocatechuic acid act as inhibitors. All divalent cations Fe2+, Mn2+, Mg2+, Cu2+ and Zn2+ stimulate the relative activity of the Santalum peroxidase at concentration of 2. 0 μM. Amino acids like L-alanine and L-valine activate the per cent relative activity, while L-proline and DL-methionine showed moderate inhibition for the Santalum peroxidase. However, a very low a concentration of cysteine acts as a strong inhibitor of Santalum peroxidase at the concentration of 0. 4 mM. Native polyacrylamide gel electrophoresis (Native-PAGE) was performed for isoenzyme determination and two bands were observed. Km and Vmax values were calculated from Lineweaver-Burk graph. The apparent Vmax/Km value for O-dianisidine and H2O2 were 400 and 5. 0 × 105 Units/min/mL respectively. © 2011 Prof. H.S. Srivastava Foundation for Science and Society.

引用

页码：153 / 159

页数：6

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