Extraction, purification and processing stability of peroxidase from plums (Prunus domestica)

• Published in: International journal of food properties 2018-01, Vol.21 (1), p.2744-2757
• Main Authors: Enachi, Elena, Grigore-Gurgu, Leontina, Aprodu, Iuliana, Stănciuc, Nicoleta, Dalmadi, Istvan, Bahrim, Gabriela, Râpeanu, Gabriela, Croitoru, Constantin
• Format: Article
• Language: English
• Subjects: Ammonium; Ammonium sulfate; Catechol; Chromatography; Enzymatic activity; enzymatic browning; Enzymes; Gel electrophoresis; Guaiacol; Hydrophobicity; inactivation kinetics; Peroxidase; pH effects; Plums; Prunus domestica; Purification; Pyrogallol; Sodium; Sodium lauryl sulfate; Sodium metabisulfite
• ISSN: 1094-2912; 1532-2386
• DOI: 10.1080/10942912.2018.1560311

Peroxidase (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 E a 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.