Purification and some properties of an Aspergillus niger beta-apiosidase from an enzyme preparation hydrolyzing aroma precursors.
J Agric Food Chem
; 47(7): 2589-93, 1999 Jul.
Article
em En
| MEDLINE
| ID: mdl-10552530
ABSTRACT
A beta-apiosidase was isolated and purified to electrophoretic homogeneity from an enzyme preparation, Klerzyme 200, through ammonium sulfate precipitation, gel filtration chromatography, ion-exchange chromatography, and HPLC on ion-exchange and size exclusion columns. The purification of the enzyme was aided by the synthesis of 4-methylumbelliferyl beta-D-apiofuranoside for the specific detection of activity on electrophoresis gels. The molecular mass estimated by SDS-PAGE was 120 kDa. The optimum activity of the beta-apiosidase was found at pH 5 and 40 degrees C. The K(m) and V(max) for p-nitrophenyl beta-D-apiofuranoside were 4.2 mM and 2460 nkat/mg of protein, respectively. The enzyme was not inhibited by glucose and ethanol. This enzyme hydrolyzed the intersugar linkages of apiofuranosylglucosides, aroma precursors from grape.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Aspergillus niger
/
Glucosidases
/
Odorantes
Idioma:
En
Revista:
J Agric Food Chem
Ano de publicação:
1999
Tipo de documento:
Article