Purification and characterization of phytase with a wide pH adaptation from common edible mushroom Volvariella volvacea (Straw mushroom).
Indian J Biochem Biophys
;
2012 Feb; 49(1): 49-54
Article
in English
| IMSEAR
| ID: sea-140218
ABSTRACT
A novel phytase with a molecular mass of 14 kDa was isolated from fresh fruiting bodies of the common edible mushroom Volvariella volvacea (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 45oC, 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.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Sepharose
/
Substrate Specificity
/
Temperature
/
Triazines
/
Enzyme Stability
/
Adaptation, Physiological
/
Chromatography, DEAE-Cellulose
/
Sequence Alignment
/
6-Phytase
/
Volvariella
Language:
English
Journal:
Indian J Biochem Biophys
Year:
2012
Type:
Article
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