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

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Ragon, Mélanie | Aumelas, André | Chemardin, Patrick | Galvez, Santiago | Moulin, Guy | Boze, Helene

Edité par CCSD ; Springer Verlag -

correspondance: boze@supagro.inra.fr. International audience. 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 Km 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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