Kiwifruit is an important export industry in New Zealand and can provide a number of health benefits to consumers.  Many of the claims for benefitting health have not been proven at the molecular level. Kiwellin, a major protein component of kiwifruit has been observed to be proteolytically cleaved in situ into two domain peptides. One peptide, kissper has shown preliminary results of having bioactive properties and may be a contributing factor to the widely known health benefits of kiwifruit consumption. Kiwellin thus represents a protein that is important for the release of a bioactive peptide, yet it is poorly characterised. Investigations into the structure of kiwellin have been made to help understand its relationship it has with kissper.

Kiwellin was purified using anion exchange and size exclusion chromatography and the structural properties were assessed by a number of analytically techniques. Kiwellin was shown to be a monomeric protein with a molecular mass of 20kDa. Small angle x-ray scattering data indicated that kiwellin is a folded, elongated protein in solution. A high melting temperature of 78oC at pH6.6 suggests a folded structure that is rigid. Further crystallography work is hoped to elucidate the folds of kiwellin and the similarities it has with kissper.