Faculty of Biology, University of Latvia
Hard copy: ISSN 1691–8088
On-line: ISSN 2255–9582
Environ Exp Biol (2016) 14: 83–90
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Environmental and

Environ Exp Biol (2016) 14: 83–90

Orginal Articles

Catalytic and kinetic properties of purified Eichhornia crassipes leaf peroxidase

Rotimi Olusanya Arise*, Bolaji Olajide Osundahunsi, Samuel Tobi Farohunbi, Abeeb Abiodun Yekeen
Department of Biochemistry, Faculty of Life Sciences, University of Ilorin, Ilorin, Nigeria
* Corresponding author, E-mail: ariserotimi@gmail.com


Peroxidase from Eichhornia crassipes leaf was purified 23.58 fold with 18.58% yield by means of (NH4)2SO4 precipitation, ion exchange and Sephadex G-75 gel filtration chromatography. Optimum temperature and substrate-dependent pH optimum for enzyme activity were 40°C and pH 4.0, 9.0 and 6.0 for 2,2’-azino-bis-(3-ethylbenzthiazolin)-6-sulfonate (ABTS), guaiacol and pyrogallol, respectively. The enzyme had high pH stability and moderate thermal stability at temperatures up to 60°C; the activation energy of inactivation of the enzyme was ~122.29 kJ mol–1. Temperature-denaturing and spontaneous recovery were shown to be time-dependent while Ca2+-enhanced recovery of the denatured enzyme was in a time-dependent manner. The enzyme showed preferential affinity for ABTS over guaiacol and pyrogallol with KM values of 31.11, 21.91 and 6.45 mM respectively. It was reversibly inhibited by Pb2+, Hg2+ and EDTA while urea only caused loss of ~30.40% activity after 60 min of incubation. E. crassipes leaf peroxidase has potential use for broad range of applications.

Key words: Eichhornia crassipes, peroxidase, pH and thermal stability, optimum temperature.

Environ Exp Biol (2016) 14: 83–90
 DOI: http://doi.org/10.22364/eeb.14.12

Prof. Gederts Ievinsh
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University of Latvia

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