Isolation and Purification of an Antifungal Protein from Kiwi Fruits and Demonstration of Its Antifungal Activity

A single polypeptide low molecular weight 25 KDa thaumatin-like antifungal protein was purified from Hayward variety of kiwifruits. It was purified to apparent homogeneity involving saline extraction, (NH4)2SO4 precipitation, anion exchange chromatography on DEAE-cellulose and gel filtration on Sephadex G-100, respectively. In present work, simple chromatography procedure was described for purifying antifungal activity form the pulp of Hayward kiwifruit. It furnishes evidence of existence of antifungal activity against Fusarium oxysporum (83.72%) and Rhizoctonia solani (33.78%) and did not show any inhibitory effect against Dematophora necatrix. The proteins have low molecular weight and would be potential importance for increasing disease resistance in plants through genetic engineering and can be used as bio control for controlling fungal diseases in plants.