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The attractive recombinant phytase from Bacillus licheniformis: biochemical and molecular characterization

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An Erratum to this article was published on 31 May 2014

Abstract

The phyL gene encoding phytase from the industrial strain Bacillus licheniformis ATCC 14580 (PhyL) was cloned, sequenced, and overexpressed in Escherichia coli. Biochemical characterization demonstrated that the recombinant enzyme has an apparent molecular weight of nearly 42 kDa. Interestingly, this enzyme was optimally active at 70–75 °C and pH 6.5–7.0. This enzyme is distinguishable by the fact that it preserved more than 40 % of its activity at wide range of temperatures from 4 to 85 °C. This new phytase displayed also a high specific activity of 316 U/mg. For its maximal activity and thermostability, this biocatalyst required only 0.6 mM of Ca2+ ion and exhibited high catalytic efficiency of 8.3 s−1 μM−1 towards phytic acid.

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Acknowledgments

The authors would like to express their gratefulness to members of the Laboratory for Biocrystallography and Structural Biology of Therapeutical Targets (CNRS/Lyon) for their generous help and support. We thank Dr Michel JUY for his kind advices and help.

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Authors and Affiliations

  1. Faculty of Sciences of Gafsa–Unit of Macromolecular Biochemistry and Genetic, Department of Life Sciences, Zarroug, 2112, Gafsa, Tunisia

    Mohamed Ali Borgi

  2. INRA, UMR 1319 Micalis, 78350, Jouy-en-Josas, France

    Samira Boudebbouze, Florette Szukala, Nicolas Pons, Emmanuelle Maguin & Moez Rhimi

  3. Laboratory for Biocrystallography and Structural Biology of Therapeutical Targets, BMSSI–Institut de Biologie et Chimie des Protéines, UMR 5086-CNRS/Université de Lyon, FR3302 “BioSciences Gerland-Lyon Sud”, 7 Passage du Vercors, 69367, Lyon cedex 07, France

    Nushin Aghajari

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  1. Mohamed Ali Borgi
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Correspondence to Moez Rhimi.

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Borgi, M.A., Boudebbouze, S., Aghajari, N. et al. The attractive recombinant phytase from Bacillus licheniformis: biochemical and molecular characterization. Appl Microbiol Biotechnol 98, 5937–5947 (2014). https://doi.org/10.1007/s00253-013-5421-9

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  • DOI: https://doi.org/10.1007/s00253-013-5421-9

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