Purification, Characterization, and Inhibition of Tyrosinase from Jerusalem Artichoke (Helianthus Tuberosus L.) Tuber.

Abstract

Background: Because it tends to cause deterioration in the quality of food and appearance, food browning is unacceptable. Tyrosinase, which catalyzes the transformation of mono phenolic compounds into o-quinones, has been associated with this phenomenon. Natural anti-browning agents were used to help avoid the enzymatic browning that occurs in many foods.

Methods: Tyrosinase of Jerusalem Artichoke tubers was purified through (NH4)2SO4 sedimentation, dialysis, chromatography, and finally gel electrophoresis. The purified enzyme was characterized and inhibited by rosemary extracts.

Results: Purification of tyrosinase from Jerusalem Artichoke tuber were accomplished. The specific activity at the final step of purification increased to 14115.76 U/mg protein with purification fold 32.89 using CM-Cellulose chromatography. The molecular mass was evaluated by electrophoresis and found to be 62 KDa. Maximum tyrosinase activity was found at 30 °C, pH 7.2, and higher affinity towards L-tyrosine. Inhibition percentage of heated extracts for leaves and flowers on tyrosinase activity was better than nonheated with 29.65% and 23.75%, respectively. The kinetic analysis exposed uncompetitive inhibition by leaves and flowers heated extracts.

Conclusion: In this study, we concluded the usage of natural anti-browning inhibitors like rosemary extract be able to be castoff to substitute the chemical agents which might be dangerous to social healthiness. Natural anti-browning agents can be used to prevent the browning of many foods.