Abstract
Peroxidases have ability to catalyze redox reaction of a wide range of phenolic as well as non-phenolic compounds and exhibited various physiological roles in plant life cycle. From the point of view of industrial applications of peroxidases, the isolation and characterization of peroxidases offering resistance to higher pH and temperature, salts, organic solvents is highly desirable. In this direction, a partial cDNA clone of peroxidase from lemon was isolated and characterized. The peroxidase was found to be defense associated as evident by the higher expression in diseased condition than that of healthy one at both the transcript and enzymatic activity levels. This defense related peroxidase from lemon leaves was purified to homogeneity using quick two step processes of heat treatment and affinity chromatography. The native peroxidase was found to be a heterotrimer of 200 kDa, consisting of two subunits each of 66 kDa while, one subunit of 70 kDa. The purified peroxidase was found to be stable towards heat (retained 92% activity at 80°C for 1 h) and organic solvents, namely ethanol, methanol and isopropanol (retained 30-50% activity in the presence of 50% (v/v) of these solvents for 1 h). Purified peroxidase also exhibited tolerance to heavy metal ions such as Cd2+, Ni2+ and Cs2+. The purified lemon peroxidase was found to efficiently oxidize the industrial dyes in the order of aniline blue>methyl orange> indigo carmine >trypan blue > crystal violet, such that 40-54% dye decolorization was observed within 4 h. Thus, the properties exhibited by purified lemon peroxidase make it a promising candidate enzyme for industrial exploitation.
Highlights
Peroxidases are one of the major H2O2 decomposing enzymes and have ability to catalyze redox reaction of a wide range of phenolic as well as non-phenolic compounds
The analyses revealed that the LPRX protein exhibited similarity with secretary peroxidases belonging to plant heme-dependent peroxidase superfamily
This defense associated peroxidase was purified to 34.40 folds with overall recovery of 54.22% through a quick purification protocol namely heat treatment and con-A affinity column chromatography
Summary
Peroxidases are one of the major H2O2 decomposing enzymes and have ability to catalyze redox reaction of a wide range of phenolic as well as non-phenolic compounds. Class I peroxidases exhibited major role in oxidative stress i.e. detoxification of ROS [6]. They include cytochrome c peroxidase, ascorbate peroxidase and catalase peroxidase. The class II peroxidases, exclusively containing fungal peroxidases, have major role in lignin biodegradation [7]. They include lignin peroxidases, manganese peroxidases and versatile peroxidases. The class III peroxidases are widely distributed in plant kingdom [8]. They include horseradish peroxidase (HRP), peanut peroxidase, soybean peroxidase, etc
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