Extraction and Purification of Vegetable Peroxidase: A Review

Abstract

Peroxidases are enzymes that catalyze the oxidation of various substrates, maintaining their enzymatic activity in wide ranges of pH and temperatures. These enzymes are used in processes for the degradation of dyes and phenolic compounds. Peroxidases are present in the tissues of several plants, and the search for new sources of this enzyme is necessary. This literature review aims to compile information about the extraction and/or purification of peroxidases contained in different plant tissues, presenting extraction methods, purification processes, enzymatic activities and their increments, according to the chemical and physical processes applied. Several plant sources can be raw material to obtain these enzymes, through different forms of extraction, where the processes of comminution predominate in the presence of buffer solution. For partial purification, are used precipitation with solvents (acetone and ethanol) and salts (ammonium sulfate) and centrifugation. For purification, chromatographic processes are used, in which molecular exclusion and affinity chromatography are prominent. It is concluded that there is a wide range of possibilities for obtaining the enzyme peroxidase from plants, with variability in the enzymatic activity when different extraction methods are applied. The purification methods used provide increases in the specific activity of the peroxidases.

Recent Advances Regarding Polyphenol Oxidase in Camellia sinensis: Extraction, Purification, Characterization, and Application

“…Chromatographic chromatography is generally used for fine purification of enzyme proteins after crude purification [54]. As shown in Table 2, the chromatographic methods used for PPO purification from tea sources mainly include ion chromatography, gel filtration chromatography, and affinity chromatography.…”