Simple Approach to Reactive Dye Decolorization Using Trichosanthes dioica Proteins at Low Concentration of 1-hydroxybenzotriazole

Enzymatic catalysis in the presence of redox mediators has emerged as an effective and feasible technique for degradation of complex structural compounds. We investigated peroxidase from Trichosanthes dioica to study decolorization of reactive dyes namely Reactive Blue15 (RB15) and Reactive Red4 (RR4) under different experimental conditions like pH, temperature, time interval, enzyme concentration and in the presence of redox mediators. Six different redox mediators; syringaldehyde, guaiacol, 1-hydroxy-benzotriazole (HOBT), vanillin, bromophenol and quinol were simultaneously evaluated. T. dioica peroxidase showed remarkable decolorization of reactive dye in the presence of 1-hydroxybenzotriazole. At an enzyme concentration of 0.45 EUmL-1 the peroxidase decolorized Reactive Red15 almost completely up to a maximum of 98.6%whereas Reactive Red4 decolorized upto 68.2%with 1.0 mM 1-hydroxybenzotriazole. Maximum decolorization was recorded at a temperature range of 40°C to 50°C at pH 5.0. Time activity plot exhibited maximum decolorization at 90 min and 180min for RB15 and RR4 respectively. It can be concluded that T. dioica peroxidase could be a potential source for developing an inexpensive and efficient method for the treatment of recalcitrant reactive dyes that are potentially toxic or even carcinogenic.