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Complete hydrolysis of myo-inositol hexakisphosphate by a novel phytase from Debaryomyces castellii CBS 2923

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Abstract

Debaryomyces castellii phytase was purified to homogeneity in a single step by hydrophobic interaction chromatography. Its molecular mass is 74 kDa with 28.8% glycosylation. Its activity was optimal at 60°C and pH 4.0. The K m value for sodium phytate was 0.532 mM. The enzyme exhibited a low specificity and hydrolyzed many phosphate esters. The phytase fully hydrolyzed myo-inositol hexakisphosphate (or phytic acid, Ins P6) to inositol and inorganic phosphate. The sequence of Ins P6 hydrolysis was determined by combining results from high-performance ionic chromatography and nuclear magnetic resonance. D. castellii phytase is a 3-phytase that sequentially releases phosphate groups through Ins (1,2,4,5,6) P5, Ins (1,2,5,6) P4, Ins (1,2,6) P3, Ins (1,2) P2, Ins (1 or 2) P1, and inositol (notation 3/4/5/6/1 or 2).

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Acknowledgments

This work was supported by ADISSEO France SAS society.

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Authors and Affiliations

  1. Equipe Génie Microbiologique et Enzymatique, SUPAGRO-INRA, 2 place Viala, 34060, Montpellier Cedex 01, France

    Mélanie Ragon, Patrick Chemardin, Santiago Galvez, Guy Moulin & Hélène Boze

  2. Centre de Biochimie Structurale, CNRS UMR 5048, INSERM U414, Université Montpellier 1, 29 rue de Navacelles, 34090, Montpellier Cedex, France

    André Aumelas

Authors
  1. Mélanie Ragon
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  2. André Aumelas
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  3. Patrick Chemardin
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  4. Santiago Galvez
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  5. Guy Moulin
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  6. Hélène Boze
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Correspondence to Hélène Boze.

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Ragon, M., Aumelas, A., Chemardin, P. et al. Complete hydrolysis of myo-inositol hexakisphosphate by a novel phytase from Debaryomyces castellii CBS 2923. Appl Microbiol Biotechnol 78, 47–53 (2008). https://doi.org/10.1007/s00253-007-1275-3

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  • DOI: https://doi.org/10.1007/s00253-007-1275-3

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