Purification and characterization of neutral invertase from chickpea nodules.
Indian J Biochem Biophys
;
1997 Dec; 34(6): 529-34
Artigo
em Inglês
| IMSEAR
| ID: sea-27962
ABSTRACT
Neutral invertase from nodules of chickpea (Cicer arietinum L.) was isolated and purified by ammonium sulphate fractionation, gel filtration and DEAE-cellulose column chromatography. The purified enzyme was stable between 0 to 40 degrees C beyond which it was irreversibly denatured. Optimum temperature and pH of the enzyme were 37 degrees C and 7.0, respectively. K(m) for sucrose was 14.2 mM and Vmax was 4.8 mumole hr-1. The enzyme was inhibited by several metal ions. From the temperature effect on K(m) and Vmax values, the energy of activation (Ea), enthalpy change (delta H) and entropy change (delta S) of the enzyme were calculated to be 147 kJmol-1, -4.10 kJmol-1 and -2.33 JK-1mol-1, respectively. By employing photo-oxidation and chemical modification and by studying the effect of pH on K(m) and Vmax, the involvement of sulphydryl-, imidazole- and alpha-amino groups in the active site of the enzyme has been indicated.
Texto completo:
DisponíveL
Índice:
IMSEAR (Sudeste Asiático)
Assunto principal:
Plantas Medicinais
/
Reagentes de Sulfidrila
/
Termodinâmica
/
Sítios de Ligação
/
Estabilidade Enzimática
/
Cinética
/
Cátions
/
Beta-Frutofuranosidase
/
Inibidores Enzimáticos
/
Glicosídeo Hidrolases
Idioma:
Inglês
Revista:
Indian J Biochem Biophys
Ano de publicação:
1997
Tipo de documento:
Artigo
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