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Characterization of three polyphenol oxidase isoforms in royal dates and inhibition of its enzymatic browning reaction by indole-3-acetic acid.
Farouk, Benaceur; Aref, Neifar; Rachid, Chaibi; Mourad, Leboukh; Emna, Ketata; Fethi, Berrabah; Rania, Bredai; Wafa, Nouioua; Kenza, Benaceur; Boumediene, Meddah; Ali, Gargouri; Hubert, Cabana; Hicham, Gouzi.
Afiliación
  • Farouk B; Laboratory of Biological and Agricultural Sciences (LSBA), Amar Thelidji University, Laghouat (UATL), 03000, Algeria. Electronic address: f.benaceur@lagh-univ.dz.
  • Aref N; Laboratory of Molecular Biotechnology of Eukaryotes, Biotechnology Center of Sfax, University of Sfax, Tunisia; Laboratory of Aqua, National Institute of Sciences and Technologies of the Sea (INSTM), Sfax, Tunisia.
  • Rachid C; Laboratory of Biological and Agricultural Sciences (LSBA), Amar Thelidji University, Laghouat (UATL), 03000, Algeria.
  • Mourad L; Laboratory of Biological and Agricultural Sciences (LSBA), Amar Thelidji University, Laghouat (UATL), 03000, Algeria.
  • Emna K; Laboratory of Molecular Biotechnology of Eukaryotes, Biotechnology Center of Sfax, University of Sfax, Tunisia.
  • Fethi B; Laboratory of Exploration and Valorization of Steppic Ecosystems, Faculty of Nature and Life Sciences, University of Ziane Achour, 17000 Djelfa, Algeria.
  • Rania B; Laboratory of Molecular Biotechnology of Eukaryotes, Biotechnology Center of Sfax, University of Sfax, Tunisia.
  • Wafa N; Department of English, Faculty of Letters and Languages, University of Laghouat, Algeria.
  • Kenza B; Laboratory of Biological and Agricultural Sciences (LSBA), Amar Thelidji University, Laghouat (UATL), 03000, Algeria.
  • Boumediene M; Laboratory of Bioconversion, Microbiological Engineering and Sanitary Security, Faculty of Sciences of Nature and Life, University of Mascaa, Road Mamounia, 29000 Mascara, Algeria.
  • Ali G; Laboratory of Molecular Biotechnology of Eukaryotes, Biotechnology Center of Sfax, University of Sfax, Tunisia.
  • Hubert C; Department of Civil Engineering, Université de Sherbrooke, 2500 Boulevard de lUniversité, Sherbrooke, Québec J1K 2R1, Canada.
  • Hicham G; Laboratory of Biological and Agricultural Sciences (LSBA), Amar Thelidji University, Laghouat (UATL), 03000, Algeria; Department of Civil Engineering, Université de Sherbrooke, 2500 Boulevard de lUniversité, Sherbrooke, Québec J1K 2R1, Canada. Electronic address: h.gouzi@lagh-univ.dz.
Int J Biol Macromol ; 145: 894-903, 2020 Feb 15.
Article en En | MEDLINE | ID: mdl-31770554
In this study, Polyphenol oxidases (PPO) from royal dates fruit was purified and characterized. These procedures led to 8-fold purification with 14.72% recovery. Three isoenzymes of royal dates PPO exhibited a molecular weight of 20.,45 and 64 kDa. The royal date PPOs had maximum activity at pH 4.6 and 8, 3.6-5.6 and 5.6 with pyrogallol, 4-methylcatechol and pyrocatechol substrates, respectively. The enzyme showed high stability in the temperature range of 30-60 °C.4-Methylcatechol was the most suitable substrate, due to the lowest Km and the biggest Vmax/Km values. The kinetic of thermal inactivation were performed in a temperature range of 60-75 °C. A biphasic model provided a good description of dates PPO thermal inactivation. Indole-3acetic acid markedly inhibited Royal dates PPO activity. Its Anti-browning effect on dates was investigated. IAA-treatment reduced weight loss, pericarp decay, browning index and membrane electrolyte leakage. Thus, a higher total anthocyanins contents and total phenolic contents was correlated with higher DPPH scavenging activity and lower MDH contents Such effect was accredited to maintain of membrane integrity and inhibition of oxidative enzymes by IAA. In conclusion, IAA could be used as a potent inhibitor of fruits enzymatic browning reaction.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Catecol Oxidasa / Isoformas de Proteínas / Frutas / Ácidos Indolacéticos Idioma: En Revista: Int J Biol Macromol Año: 2020 Tipo del documento: Article Pais de publicación: Países Bajos
Texto completo
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Imprimir
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Catecol Oxidasa / Isoformas de Proteínas / Frutas / Ácidos Indolacéticos Idioma: En Revista: Int J Biol Macromol Año: 2020 Tipo del documento: Article Pais de publicación: Países Bajos