Extraction, purification and processing stability of peroxidase from plums (Prunus domestica)
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 estima...
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doaj-2a4a6385e5fe4b34909833db5c4d3f282020-11-24T21:20:57ZengTaylor & Francis GroupInternational Journal of Food Properties1094-29121532-23862018-01-012112744275710.1080/10942912.2018.15603111560311Extraction, purification and processing stability of peroxidase from plums (Prunus domestica)Elena Enachi0Leontina Grigore-Gurgu1Iuliana Aprodu2Nicoleta Stănciuc3Istvan Dalmadi4Gabriela Bahrim5Gabriela Râpeanu6Constantin Croitoru7Dunarea de Jos University of GalatiDunarea de Jos University of GalatiDunarea de Jos University of GalatiDunarea de Jos University of GalatiSzent István UniversityDunarea de Jos University of GalatiDunarea de Jos University of GalatiThe Academy of Agricultural and Forestry SciencesPeroxidase (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.http://dx.doi.org/10.1080/10942912.2018.1560311Plumsperoxidaseenzymatic browninginactivation kinetics |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Elena Enachi Leontina Grigore-Gurgu Iuliana Aprodu Nicoleta Stănciuc Istvan Dalmadi Gabriela Bahrim Gabriela Râpeanu Constantin Croitoru |
spellingShingle |
Elena Enachi Leontina Grigore-Gurgu Iuliana Aprodu Nicoleta Stănciuc Istvan Dalmadi Gabriela Bahrim Gabriela Râpeanu Constantin Croitoru Extraction, purification and processing stability of peroxidase from plums (Prunus domestica) International Journal of Food Properties Plums peroxidase enzymatic browning inactivation kinetics |
author_facet |
Elena Enachi Leontina Grigore-Gurgu Iuliana Aprodu Nicoleta Stănciuc Istvan Dalmadi Gabriela Bahrim Gabriela Râpeanu Constantin Croitoru |
author_sort |
Elena Enachi |
title |
Extraction, purification and processing stability of peroxidase from plums (Prunus domestica) |
title_short |
Extraction, purification and processing stability of peroxidase from plums (Prunus domestica) |
title_full |
Extraction, purification and processing stability of peroxidase from plums (Prunus domestica) |
title_fullStr |
Extraction, purification and processing stability of peroxidase from plums (Prunus domestica) |
title_full_unstemmed |
Extraction, purification and processing stability of peroxidase from plums (Prunus domestica) |
title_sort |
extraction, purification and processing stability of peroxidase from plums (prunus domestica) |
publisher |
Taylor & Francis Group |
series |
International Journal of Food Properties |
issn |
1094-2912 1532-2386 |
publishDate |
2018-01-01 |
description |
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 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. |
topic |
Plums peroxidase enzymatic browning inactivation kinetics |
url |
http://dx.doi.org/10.1080/10942912.2018.1560311 |
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