Purification and identification of a phytase from fruity bodies of the winter mushroom, Flammulina velutipes

A phytase, with a molecular mass of 14.8 kDa as determined by gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis was isolated from fresh fruiting bodies of the mushroom Flammulina velutipes. The chromatographic procedure used for isolation of the phytase included ion exchan...

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Bibliographic Details
Published in:African journal of biotechnology 2011-12, Vol.10 (77), p.17845-17852
Main Authors: Zhu, MJ, Wang, H X, Ng, T B
Format: Article
Language:English
Subjects:
Flammulina velutipes
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Summary:A phytase, with a molecular mass of 14.8 kDa as determined by gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis was isolated from fresh fruiting bodies of the mushroom Flammulina velutipes. The chromatographic procedure used for isolation of the phytase included ion exchange chromatography on DEAE-cellulose, CM-cellulose, Q-Sepharose, affinity chromatography on Affi-gel blue gel and fast protein liquid chromatography-gel filtration on Superdex 75. The enzyme was adsorbed on DEAE-cellulose, unadsorbed on CM-cellubse and Affi-gel blue gel, and adsorbed on Q-Sepharose. It presented an N-terminal sequence different from those of reported fungal phytases. It exhibited maximal activity at about 45 degree C and it did not manifest drastic fluctuations in activity over the pH of 3 to 9. The phytase presented activity towards a variety of phosphorylated compounds with the following ranking of activity: ATP > fructose-6-phosphate approximately glucose-6-phosphate > AMP > ADP> beta -glycerophosphate > sodium phytate. It did not present antifungal activity.
ISSN:1684-5315
1684-5315
DOI:10.5897/AJB10.2625