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|Title:||Purification and characterization of phytase with a wide pH adaptation from common edible mushroom <i style="">Volvariella volvacea</i> (Straw mushroom)|
Ng, Tzi Bun
<i style="">Volvariella Volvacea</i>
|Abstract:||A novel phytase with a molecular mass of 14 kDa was isolated from fresh fruiting bodies of the common edible mushroom <i style="">Volvariella volvacea</i> (Straw mushroom). The isolation procedure involved successive chromatography on DEAE-cellulose, CM-cellulose, Affi-gel blue gel, Q-Sepharose and Superdex-75. The enzyme was a monomeric protein and was unadsorbed on DEAE-cellulose, CM-cellulose and Affi-gel blue gel, but was adsorbed on Q-Sepharose. The enzyme was purified 51.6-fold from the crude extract with 25.9% yield. Its N-terminal amino acid sequence GEDNEHDTQA exhibited low homology to the other reported phytases. The optimal pH and temperature of the purified enzyme was 5 and 45<sup>o</sup>C, respectively. The enzyme was quite stable over the pH range of 3.0 to 9.0 with less than 30% change in its activity, suggesting that it can be used in a very wide pH range. The enzyme exhibited broad substrate selectivity towards various phosphorylated compounds, but lacked antifungal activity against tested plant pathogens.|
|ISSN:||0975-0959 (Online); 0301-1208 (Print)|
|Appears in Collections:||IJBB Vol.49(1) [February 2012]|
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