Laboratory for Public Health Biotechnology, Box 8094, University of Yaoundé I, Yaoundé, Cameroon.
Research Article
World Journal of Advanced Research and Reviews, 2021, 12(03), 476–483
Received on 14 November 2021; revised on 23 December 2021; accepted on 25 December 2021
Several soluble peroxidase isoenzymes are expressed in a landrace of Vigna sp. cultivated in the north of Cameroon (landrace called Vn in previous study) during seed germination. There are at least two cathodic peroxidases and eight major anodic peroxidases as shown by their electrophoretic migration at pH 7.4 under native conditions. These isoperoxidases are more expressed in roots than in shoots. They have different thermal stability, so that heat inactivation kinetics of crude peroxidase extracts from roots do not fit the first-order model. The slow and intermediate migrating groups of anodic isoperoxidases retains a substantial activity after ten minutes of incubation at 80°C and 85°C. An anodic isoperoxidase (named A6 in this study) shows in addition to this great thermal stability, a high activity in seedlings and is expressed both in roots and shoots. The combination of those characteristics makes this isoperoxidase a potential candidate for biotechnological applications. Three major anodic isoperoxidases, of which A6 and another thermostable isoperoxidase, were successfully separated from each other by ion exchange chromatography on DEAE-cellulose, after precipitation of total proteins by ice-cold acetone. This offers the prospect of being able to characterize these isoperoxidases individually in future studies.
Peroxidase; Vigna; Isoenzymes; Thermal stability; Purification
Preview Article PDF
Yves Mann Elate Lea Mbassi, Marie Solange Evehe, Wilfred Fon Mbacham and John Payne Muluh. Identification and partial purification of thermally stable peroxidase isoenzymes from seedlings of Vigna sp. (V) landrace Vn. World Journal of Advanced Research and Reviews, 2021, 12(3), 476-483. Article DOI: https://doi.org/10.30574/wjarr.2021.12.3.0706