| Autor: |
Arise, Rotimi Olusanya, Osundahunsi, Bolaji Olajide, Farohunbi, Samuel Tobi, Yekeen, Abeeb Abiodun |
| Předmět: |
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| Zdroj: |
Environmental & Experimental Biology; 2016, Vol. 14 Issue 2, p83-90, 8p |
| Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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