Further characterization of phytase from Phaseolus aureus

Maiti, I. B. ; Biswas, B. B. (1979) Further characterization of phytase from Phaseolus aureus Phytochemistry, 18 (2). pp. 316-318. ISSN 0031-9422

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/003194...

Related URL: http://dx.doi.org/10.1016/0031-9422(79)80079-5


Phytase purified to homogeneity from germinated mungbean cotyledons was inhibited by EDTA although it did not show any absolute requirement for divalent cations. Sodium fluoride, sodium citrate, mercaptoethanol and pCMB also inhibit the phytase activity but L-phenylalanine has no effect on activity. The phytase has a low affinity for inositol monophosphate. The relative rate of dephosphorylation of myo-inositol-1-phosphate and myo-inositol-5 phosphate by phytase is 6 and 18% respectively of that of myo-inositol-hexaphosphate. Mungbean phytase cannot cleave myo-inositol-2-phosphate, 1,2-cyclic inositol phosphate, Na-β -glycerophosphate or p-nitrophenylphosphate. The relative rates of hydrolysis of different isomers of inositol hexaphosphate are in the following order: myo-IP6, > neo-IP6 > scyllo-IP6 = D-chiro-IP6, > L-chiro-IP6. This enzyme seems to be most active with myo-inositol hexaphosphate.

Item Type:Article
Source:Copyright of this article belongs to Phytochemical Society of Europe.
Keywords:Phaseolus aureus; Leguminosae: Mungbean; Phytase: Myoinositol Phosphates
ID Code:3512
Deposited On:12 Oct 2010 04:22
Last Modified:18 May 2011 11:44

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