An antifungal protein with a molecular mass of 38.6 kDa was isolated from the seed of Prosopis cineraria. The protein was purified using ammonium sulphate precipitation, ion exchange chromatography and gel filtration. The antifungal activity of purified protein was retained up to 50 °C for 10 min. The MALDI TOF mass spectroscopy revealed 15 assorted peptides. The molecular weight of the antifungal protein is different from antifungal proteins reported in seeds of other leguminous plants. The purified protein exerted antifungal activity against post-harvest fruit fungal pathogens Lasiodiplodia theobromae and Aspergillus fumigatus, isolated from the rotten fruits. The antifungal properties of this novel antifungal protein can be potentially exploited to manage post-harvest fungal disease of fruits through alternative means to reduce use of hazardous chemicals.
Keywords: Antifungal protein; ITS-5.8S gene; Ion-exchange chromatography; MALDI-TOF MS/MS; Thermostability.
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