Abstract

Rhodanese a ubiquitous sulphur transferase enzyme catalyses the detoxification of cyanide to a less toxic thiocyanate. Rhodanese from the root of Pentadiplandra brazzeana was purified by ammonium sulphate precipitation and affinity chromatography. The enzyme had a specific activity of 4.82 RU/mg of protein. The Km values of the substrates (KCN and Na2S2O3) were 11.76 and 10 mM, respectively. The optimum pH and temperature of the enzyme activity were 8.0 and 60°C, respectively. The enzyme was not inhibited by the heavy metals (BaCl2, KCl, NiCl2, NaCl, MnCl2, and ZnCl2). This study affirmed the presence of rhodanese in the root of P. brazzeana, an indication that the plant may be of useful biotechnological application, especially in bioremediation of cyanide intoxified farm sites.   Key words: Cyanide, rhodanese, detoxification, inhibition, Pentadiplandra brazzeana.

Highlights

  • Rhodanese is a multifunctional, mitochondrial sulphur transferase enzyme that catalyses the detoxification of cyanide by sulphuration in a double displacement mechanistic reaction (Smith and Urbanska, 1986)

  • A close relationship exists between rhodanese activity and cyanogenesis, which suggests that the enzyme provides a mechanism for cyanide detoxification in cyanogenic plants (Smith and Urbanska, 1986)

  • It is widely believed that the major function of rhodanese is in cyanide detoxification, according to Okonji and Agboola (2014), the wide distribution of rhodanese in different tissues is an indication that there may be other functions

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Summary

Introduction

Rhodanese (cyanide: thiosulphate sulphur transferase; E.C.2.8.1.1) is a multifunctional, mitochondrial sulphur transferase enzyme that catalyses the detoxification of cyanide by sulphuration in a double displacement (ping pong) mechanistic reaction (Smith and Urbanska, 1986). The presence of rhodanese enzyme in the root of P. brazzeana (Baill), a plant common in the Eastern part of Nigeria used mostly as spicing ingredient in food preparation is reported in this study. The kinetic constants of the P. brazzeana root rhodanese were determined in the presence of two other sources of sulphur, namely; (NH4)2S2O8 and Na2S2O5 at concentrations varied between 25 and 250 mM and at a fixed concentration of 250 mM KCN, respectively.

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