The beginning study of transglutaminase from plant origin

Agricultural Industrial Technology, Trunojoyo University Madura (UTM), East Java, Indonesia
Biology Department, University of Muhammadiyah Malang (UMM), East Java, Indonesia

^* Corresponding author: wahyuprihanta@gmail.com

Abstract

Texture is an important parameter in processed foods such as meatball, sausage and surimi, where it is affected by the protein gel strength. Sodium tripolyphosphate is often used to improve quality of food texture, and even borax which is harmful to health including causing severe dizziness and trouble breathing, is still widely used. This study aims to explore and characterize transglutaminase of plant origin which is safer than gelling chemicals agents in food products. Transglutaminase is an enzime that can modify protein into strong gel by creating cross-linkage among protein chains. Animal tissue is one source of transglutaminase but requires high costs for providing raw materials. While the search for transglutaminase source from microorganisms need many stages to ensure that transglutaminase meets safety standards, therefore transglutaminasefrom plant origin is an alternative. The method in this study was to identify and characterize transglutaminase extracted from iodine leaf (Jatropha multifida), including determining the optimum temperature, optimum pH as well as activator and inhibitor of transglutaminase extract from iodine leaf. The results showed that the optimum temperature for transglutaminase from iodine leaf is 40-60 ^oC; The optimum pH is in the range of 6-7. Unlike most transglutaminases derived from animal tissues, transglutaminase from iodine leaf does not depent on presence of Ca^2+, however Zn²⁺ could be an inhibitor. Transglutaminase extract from iodine leaf has high activity, it will be a promising potential to be applied in food industry to improve texture quality.