Purification and characterization of a phytate-degrading enzyme from germinated faba beans (Vicia faba Var. Alameda)

A phytate-degrading enzyme was purified ∼2190-fold from germinated 4-day-old faba bean seedlings to apparent homogeneity with a recovery of 6% referred to the phytase activity in the crude extract. It behaves as a monomeric protein of a molecular mass of ∼65 kDa. The phytate-degrading enzyme belongs to the acidic phytases. It exhibits a single pH optimum at 5.0. Optimal temperature for the degradation of sodium phytate is 50 °C. Kinetic parameters for the hydrolysis of sodium phytate are KM = 148 μmol L-1 and kcat = 704 s-1 at 35 °C and pH 5.0. The faba bean phytase exhibits a broad affinity for various phosphorylated compounds and hydrolyzes phytate in a stepwise manner. The first hydrolysis product was identified as D/L-myo-inositol(1,2,3,4,5)pentakisphosphate.

Bibliographic Details

Main Authors:	Greiner, R., Muzquiz, M., Burbano, C., Cuadrado Hoyos, María Carmen, Pedrosa, M. M., Goyoaga, C.
Format:	artículo biblioteca
Language:	English
Published:	American Chemical Society 2001
Subjects:	Legume phytase, Myo-inositol phosphate phosphohydrolase, Phytate degradation,
Online Access:	http://hdl.handle.net/20.500.12792/1982 http://hdl.handle.net/10261/290775
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