Sapodilla rTLP exists as a monomer, dimer with β-1, 3-glucanase and antifungal activity.

The present study deals in understanding the structure-function relationship of Sapodilla thaumatin-like protein (TLP). Most of the TLPs known to be stimulated in response to biotic, and abiotic stress. Few TLPs possess both antifungal and enzymatic properties, only very few TLPs possess either of the activity or none of the attributes. This characteristic of TLPs offer great challenges to examine its functional differences among its members, though they are structurally homologous. Therefore, we were concerned to see the functionality of Sapodilla TLP, by cloning in E. coli, expression, purification, and characterization. Being a plant derived protein, it possesses post-translational modifications such as the presence of disulfide bonds. Hence, we proposed to adapt various protein purification tools to purify and to obtain biologically active protein. The refolded and purified rTLP (recombinant TLP) exists as a monomer and dimer with {beta}-1, 3-glucanase, and antifungal activity. The structure, function, relationship studies of rTLP (through deletion and site directed mutagenesis), observed to knock out the dimeric nature. Lastly, structural bioinformatics of rTLP reveal that their primary structural types are - {beta}- and non-helical structures.