Enhanced stability of crude protease from kiwifruit (Actinidia deliciosa) by adding hydrocolloid for organic processed food uses

Abstract

ABSTRACTCrude protease originating from kiwifruit (Actinidia deliciosa) was extracted for organic processed food uses. The protease included in the kiwifruit can be utilized for organic uses instead of current commercial enzymes from microbial origin, which are not suitable for organic processed food. Crude protease extracted by physical treatment rather than any biochemical purification methods was appropriate for the organic processed food uses. However, crude protease extract has been found to be unstable for processing and storage usage, which has to be modified to be stable by appropriate methods suitable for organic processed food uses. The proteolytic activity of the protease extracted from kiwifruit was measured using casein as a substrate. The decreased inactivation rate constant of crude protease treated with guar gum and locust bean gum within the temperature range of 30–50°C implied the enhanced stability of crude enzymes by treatment with hydrocolloid. The half-times of crude proteases treated with guar gum and locust bean gum were higher than the half-time of native crude protease at 40°C (optimum temperature of the native crude protease), with values of 55.45 min for the guar gum-treated sample, 50.23 min for the locust bean gum-treated sample and 23.26 min for the native sample, demonstrating the quantitative evidence of the enzyme stability. The relatively stable maintenance of the proteolytic activity has helped to realize hydrocolloid-treated enzyme to be used for hydrolytic function in organic processed food applications.