Complete hydrolysis of <Emphasis Type="Italic">myo</Emphasis>-inositol hexakisphosphate by a novel phytase from <Emphasis Type="Italic">Debaryomyces castellii</Emphasis> CBS 2923 |
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Authors: | Mélanie Ragon André Aumelas Patrick Chemardin Santiago Galvez Guy Moulin Hélène Boze |
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Institution: | (1) Equipe Génie Microbiologique et Enzymatique, SUPAGRO-INRA, 2 place Viala, 34060 Montpellier Cedex 01, France;(2) Centre de Biochimie Structurale, CNRS UMR 5048, INSERM U414, Université Montpellier 1, 29 rue de Navacelles, 34090 Montpellier Cedex, France |
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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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Keywords: | Debaryomyces castellii Yeast Phytase Enzyme characterization Inositol phosphates Phytate degradation NMR HPIC |
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