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Partial purification and characterization of phytases from pollen of lily (Lilium longiflorum Thunb.)

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Summary

Two phytases from lily pollen (Lilium longiflorum Thunb.) were partially purified and characterized. The first (pH optimum 5.0) was purified 40-fold from ungerminated pollen. The second (pH optimum 6.5) appeared during germination and was purified 68-fold from pollen germinated 2 h. Molecular weight of the first was 72 kD, and the second was 36 kD as determined by gel filtration. Both were active against phosphate esters other than phytate, although purification of the first reduced its activity against AMP and myo-inositol 2-P to 10% of activity against phytate. Phytase from germinated pollen (but not ungerminated) was inhibited by the sulfhydryl agent parahydroxy mercuribenzoate; P i inhibited phytase from ungerminated but not germinated pollen. Such different catalytic and physical properties may reflect different biochemical functions.

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Abbreviations

HPLC:

High performance liquid chromatography

DEAE:

diethyl aminoethyl

P i :

orthophosphate

PP i :

pyrophosphate

p-NPP:

para-nitrophenyl phosphate

pNP:

para-nitrophenol

MI:

myo-inositol

MI 2-P:

myo-inositol 2-P

MI penta P:

myo-inositol pentakisphosphate

PHMB:

para-hydroxy mercuribenzoate

PMSF:

phenyl methyl sulfonyl fluoride

AMP:

adenosine monophosphate

GMP:

guanosine monophosphate

EGTA:

ethylene glycol-bis (β-aminoethyl ether) N, N, N′, N′-tetraacetic acid

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Lin, JJ., Dickinson, D.B. & David Ho, TH. Partial purification and characterization of phytases from pollen of lily (Lilium longiflorum Thunb.). Plant Cell Reports 9, 211–215 (1990). https://doi.org/10.1007/BF00232182

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  • DOI: https://doi.org/10.1007/BF00232182

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