Published January 1, 2018
| Version v1
Journal article
Open
Purification of peroxidase from Amsonia orientalis by three-phase partitioning and its biochemical characterization
- 1. Kocaeli Univ, Fac Arts & Sci, Dept Biol, TR-41380 Kocaeli, Turkey
- 2. Kocaeli Univ, Fac Arts & Sci, Dept Chem, Kocaeli, Turkey
Description
The present work describes the purification and characterization of peroxidase from the medicinal plant, Amsonia orientalis, for the first time. The activity recovery for peroxidase was 162% with 12.5-fold purification. Optimal purification parameters were 20% (w/v) (NH4)(2)SO4 saturation at pH 6.0 and 25 degrees C with 1.0:1.0 (v/v) ratio of crude extract to t-butanol ratio for 30 min. The molecular mass of the enzyme was found to be ca. 59 kDa. Peroxidase showed K-m values of 1.88 and 2.0 mM for pyrogallol and hydrogen peroxide, respectively. FeSO4, CuSO4, HgCl2, MnSO4 and MgSO4 did not inhibit the enzyme activity.
Files
bib-027ff8ed-56c5-4569-88ef-6103a0462b86.txt
Files
(220 Bytes)
| Name | Size | Download all |
|---|---|---|
|
md5:a9dbb2d8663722122984d5c686129424
|
220 Bytes | Preview Download |