Abstract
ABSTRACTPeroxidase (POD) was extracted from Prunus domestica and partially purified by three methods: ammonium sulfate precipitation, hydrophobic interaction chromatography, and ion exchange chromatography, respectively. The selected procedure allowed a 26.33-fold purification, and the molecular mass estimated by SDS-PAGE was 58 kDa. The purified enzyme presented enzymatic activity toward guaiacol, pyrogallol, catechol, and showed no activity toward ferulic, caffeic, and p-coumaric acids. In terms of optimum parameters for activity, the pH was 6.5, whereas the temperature was 25°C. The enzyme exhibited high stability in the pH range of 5.0–7.0 and in the temperature range of 25–70°C. The most potent inhibitors of POD were L-cysteine and sodium metabisulfite. The thermal inactivation displayed a first-order kinetic model, with an activation energy of Ea 84.79 ± 2.2 kJ/mol. POD extracted from plums exhibited high stability at high-pressure treatment, maintaining over 50% of the initial activity even at 700 MPa.
Highlights
Fruits and vegetables are of great importance in terms of nutrition and functional quality of fresh or processed products, providing essential biologically active compounds, which are known for their health benefits
Our results are in contradiction with the studies of Cai et al.[17] who purified the peroxidase from Jatropha curcas leaves and reported that after the final purification step, a 216-fold was achieved with a yield of 37.6%
In accordance with the specific enzymatic activity values, the results suggested the presence of both enzymes, polyphenol oxidase (PPO)[8] and POD, corresponding to the two protein bands separated by SDS-PAGE
Summary
Fruits and vegetables are of great importance in terms of nutrition and functional quality of fresh or processed products, providing essential biologically active compounds, which are known for their health benefits. POD catalyzes the oxidation of several compounds such as phenols, aromatic amines, ascorbic acid, indole, in the presence of hydrogen peroxide as an electron acceptor.[3] Plant PODs belong to Class III PODs, being involved in several processes of plant growth, including cell wall metabolism, lignification, defense against pathogens, wound healing, plant maturation Their ability to catalyze various redox reactions for a wide range of substrates highlights POD as being one of the most important industrial enzymes with applications in different industrial sectors, such as bioremediation, synthetic dye decolorization, polymer synthesis, biosensor development for diagnostic kit – ELISA[4], degradation of wastewater and drinking water, and preparation of detergents.[5] POD is one of the main quality deterioration indicator, such as flavor loss and different biodegradation reactions, being relevant as a browning enzyme that contributes to the darkening of fruit and vegetable products during processing and storage.[6]
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