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Purification and characterization of an amylase from Opuntiaficus-indica seeds

Authors

  • Monia Ennouri,

    Corresponding author
    1. Higher Institute of Applied Sciences and Technology of Mahdia, Sidi Messaoud 5111Mahdia, Tunisia
    2. Alimentary Analysis Unit, National Engineering School of Sfax, 3038 Sfax, Tunisia
      Monia Ennouri, (ISSAT) Higher Institute of Applied Sciences and Technology ofMahdia, SidiMessaoud 5111 Mahdia, Tunisia. E-mail: monia.ennouri@enis.rnu.tn
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    • These authors participated equally to the work.

  • Bassem Khemakhem,

    1. Laboratory of Plant Biotechnology, Faculty of Sciences Sfax, 3000 Sfax, Tunisia
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    • These authors participated equally to the work.

  • Hanen Ben Hassen,

    1. Laboratory of Microorganisms and Biomolecules, Molecular and Cellular Screening Research Group, Center of Biotechnology of Sfax, University of Sfax, 3018 Sfax, Tunisia
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  • Imen Ammar,

    1. Alimentary Analysis Unit, National Engineering School of Sfax, 3038 Sfax, Tunisia
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  • Karima Belghith,

    1. Laboratory of Plant Biotechnology, Faculty of Sciences Sfax, 3000 Sfax, Tunisia
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  • Hamadi Attia

    1. Alimentary Analysis Unit, National Engineering School of Sfax, 3038 Sfax, Tunisia
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Monia Ennouri, (ISSAT) Higher Institute of Applied Sciences and Technology ofMahdia, SidiMessaoud 5111 Mahdia, Tunisia. E-mail: monia.ennouri@enis.rnu.tn

Abstract

BACKGROUND: In Tunisia, prickly pear fruit grow spontaneously; it is consumed as fresh fruit, juice or jam. When the fruit is used for juice production, the seeds are discarded and go to waste. Our study aimed to extract biomolecules from seeds by producing value-added products from the fruits.

RESULTS: An amylase from Opuntia ficus-indica seeds was extracted and purified to homogeneity. An increase in specific activity of 113-fold was observed. The apparent molecular mass of the enzyme is 64 kDa. The optimum pH and temperature for enzyme activity were pH 5 and 60 °C, respectively. Under these conditions, the specific activity is 245.5 U mg−1. The enzyme was activated by Co2+ and Mg2+ (relative activity 117% and 113% respectively) at lower ion concentrations. It was strongly inhibited by Mn2+ and Fe2+. Cu2+ inhibited totally the activity of this enzyme, but Ca2+ has an inhibitory effect which increases with ion concentration.

CONCLUSION: The extracted enzyme belongs to the exo type of amylases and is classified as a β-cyclodextrin glycosyltransferase since it generates mainly β-cyclodextrin from starch. It exhibits high thermal stability and a broad range of pH stability, making it a promising prospect for industrial and food applications. Copyright © 2012 Society of Chemical Industry

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