Purification and Characterization of Arginase from the Stomach of Cane rat (Thryonomys swinderianus, Temminck 1827)

Agboola, Oluwaseun Emmanuel; Adewole, Scholes Taiwo; Ilesanmi, Olutosin Samuel

doi:10.30491/jabr.2021.268720.1343

Purification and Characterization of Arginase from the Stomach of Cane rat (Thryonomys swinderianus, Temminck 1827)

Document Type : Original Article

Authors

Oluwaseun Emmanuel Agboola ¹

Scholes Taiwo Adewole ²

Olutosin Samuel Ilesanmi ³

¹ Department of Biochemistry and Molecular Biology, Obafemi Awolowo University, Ile-Ife, Osun State, Nigeria

² Department of Chemical Sciences, Kings University, Odeomu, Osun State, Nigeria

³ Department of Chemical Sciences, Achievers University, Owo, Nigeria

10.30491/jabr.2021.268720.1343

Abstract

Introduction: Rodent pests are unique threats to agriculture and food security in many developing countries. Hence, this study investigated some physicochemical properties of partially purified arginase from the stomach of cane rats (Thryonomys swinderianus). This was with a view to understanding the significance of the enzyme in nitrogen metabolism, which could be exploited in the control of rodent pests.
Materials and Methods: Arginase was isolated and subjected to 70% ammonium sulfate (NH₄)₂SO₄ precipitation and dialyzed. The dialysate was further purified using ion-exchange chromatography on CM-Sephadex C-50 matrix.
Results: Apparent Km of the enzyme for L-arginine and Vmax were 54 ± 0.7 mM and 0.057 ± 0.1 μmol/minute/ml, while the optimum pH and temperature obtained for the enzyme were 7 and 70 °C, respectively. NaCl, MnCl₂, and HgCl₂activated the enzyme activity, while FeCl₃ totally inactivated the enzyme at tested concentrations. β-mercaptoethanol, urea, and EDTA profoundly potentiated the activity of the enzyme. Enzyme activity (81%) was retained when arginine was substituted with cysteine, while histidine, proline, alanine, tyrosine, and tryptophan had potent inhibitory effects on the enzyme activity.
Conclusions: The study established the presence of arginase in the stomach of cane rat and illuminated some physicochemical properties of the enzyme, which could be exploited in its deployment as a viable strategy to control T. swinderianus. However, further studies including structure-function investigations of the enzyme are recommended to fully exploit its potential in the control of rodent pests.

Keywords

Arginase

Arginine

Cane Rat

Enzyme