A study of superoxide dismutase activity and superoxide production in kiwifruit

Abstract

The activity of superoxide dismutase (SOD) was determined in three kiwifruit (Actinidia) species including A. deliciosa, A. chinensis, and A. arguta. Among the species tested, the highest SOD activity was found in crude extracts prepared from fruit tissues of A. deliciosa. The highest enzyme activity was localized in seed, followed by locules, core and outer pericarp (OP). SOD activity in crude extract of whole fruit remained stable for at least one month when stored at -20℃. The effect of synthetic protease inhibitors (PI) on SOD activity was investigated. Supplementing crude kiwifruit extracts with PI improved SOD activity in freshly prepared extracts, and in extracts stored at 4℃, but had no effect on those stored at -20℃. Among the PI used, iodoacetamide (an inhibitor of cysteine proteases, for example, actinidin which is a principal protease found in kiwifruit) and PMSF (an inhibitor of serine proteases), had the most and least influence on SOD activity in crude kiwifruit extracts, respectively. There was a significant increase in SOD activity in kiwifruit (that were relatively firm) when the fruits were stored at low temperature (4℃). An increase in SOD activity was also correlated with a decrease in fruit firmness. Staining fruit tissues with nitroblue tetrazolium (NBT) provided evidence for stress-induced superoxide generation in kiwifruit tissues. Taken together, the changes in SOD activity and the capacity for stress-inducible superoxide production in post-harvest kiwifruit suggest that SOD might play a fundamental role in the storage life/ripening of kiwifruit.