The attractive recombinant phytase from Bacillus licheniformis: biochemical and molecular characterization - INRAE - Institut national de recherche pour l’agriculture, l’alimentation et l’environnement Access content directly
Journal Articles Applied Microbiology and Biotechnology Year : 2014

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

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 Ca(2+) ion and exhibited high catalytic efficiency of 8.3 s(-1) μM(-1) towards phytic acid.
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Dates and versions

hal-03371033 , version 1 (08-10-2021)

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Mohamed Ali Borgi, Samira Boudebbouze, Nushin Aghajari, Florette Szukala, Nicolas Pons, et al.. The attractive recombinant phytase from Bacillus licheniformis: biochemical and molecular characterization. Applied Microbiology and Biotechnology, 2014, 98 (13), pp.5937-5947. ⟨10.1007/s00253-013-5421-9⟩. ⟨hal-03371033⟩
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