Phytase from Klebsiella Sp. No. PG-2: purification and properties.
Indian J Biochem Biophys
;
1990 Apr; 27(2): 98-102
Artículo
en Inglés
| IMSEAR
| ID: sea-28202
ABSTRACT
A phytase (EC 3.1.3.8) was extracted from rat intestinal bacterium, Klebsiella Sp. No. PG.-2, and purified 50-fold by ammonium sulphate fractionation, ion-exchange chromatography and gel filtration. The enzyme is inducible in nature. The pH optimum was at 6.0 for all the inositol phosphates studied and this characterized the enzyme as an acid phosphohydrolase. Of a range of potential substrates tested, only p-nitrophenyl phosphate alongwith the inositol phosphates was hydrolyzed. It exhibits a Km of 2.0 mM; temperature optimum of 37 degrees C and energy of activation 9,120 cal/mole for all the inositol phosphates studied. The activity was inhibited by Ag2+, Hg2+, Cu2+, fluoride and high substrate concentration.
Texto completo:
Disponible
Índice:
IMSEAR (Asia Sudoriental)
Asunto principal:
6-Fitasa
/
Klebsiella
Idioma:
Inglés
Revista:
Indian J Biochem Biophys
Año:
1990
Tipo del documento:
Artículo
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