Purification and characterization of a novel thermostable antifungal protein with chitinase activity from mung bean

Abstract

Aim: Antifungal proteins are produced by many plant species and participate in defence mechanisms against number of fungal pathogens. The main objective of the study was to purify and characterize the thermo-stable antifungal compound with chitinase activity from mung bean Vigna radiata seeds to assess their antifungal potency. Methodology: The antifungal protein was isolated through ammonium sulphate precipitation method followed by its purification through ion-exchange chromatography. The purified protein was characterized by evaluating its antifungal efficacy, thermal stability, chitinase activity and SDS PAGE profiling. Results: Molecular mass of characterized antifungal protein was 50.6 kDa. Purified protein exhibited antifungal activity against pathogenic fungi Macrophomina phaseolina and Magnaporthe grisea and sustained its thermo-stability up to 60°C with chitinase activity. Interpretation: The isolated antifungal proteins showed unique column chromatographic behaviour, molecular weight, specificity of chitinase activity and relatively high thermo-stability with potent antifungal activity. It can be used in different biomedical and pharmaceutical applications as bio-pesticides.