ß-Galactosidase from Aspergillus niger: Separation and characterization of 3 multiple forms

Détails

Ressource 1Demande d'une copie Sous embargo indéterminé.
Etat: Public
Version: de l'auteur
ID Serval
serval:BIB_08D633FBC6B9
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
ß-Galactosidase from Aspergillus niger: Separation and characterization of 3 multiple forms
Périodique
European Journal of Biochemistry
Auteur(s)
Widmer F., Leuba J.L.
ISSN
0014-2956
Statut éditorial
Publié
Date de publication
1979
Peer-reviewed
Oui
Volume
100
Numéro
2
Pages
559-567
Langue
anglais
Résumé
The enzyme ß-galactosidase (EC 3.2.1.23) from Aspergillus niger was purified and resolved into three multiple forms, using molecular sieving, ion-exchange, an hydrophobic chromatography. The isolated enzyme forms accounted for 83%, 8%, and 9% of the total ß-galactosidase activity, respectively. They were glycoproteins with estimated molecular weights of 124,000, 150,000 and 173,000, isoelectric points of about 4.6, and pH optima between 2.5 and 4.0. Amino acid and carbohydrate analyses showed that multiplicity was mainly due to dissimilar carbohydrate contents (about 12.5%, 20.5% and 29% neutral carbohydrates, respectively). The multiple form pattern might depend on the culture conditions. The ß-galactosidase forms were heat-stable up to about 60 degrees C. The Km values for lactose ranged from 85 mM to 125 mM, whereas those for the synthetic substrate o-nitrophenyl-ß-D-galactopyranoside were equal to about 2.4 mM. The V values obtained at 30 degrees C for lactose and o-nitrophenyl-ß-D-galactopyranoside were 104 units/mg enzyme protein and 121 units/mg enzyme protein, respectively (weighted averages for the three enzyme forms). The slight reactional dissimilarities between the three enzyme forms are unlikely to be physiologically relevant. The biological significance of A. niger ß-galactosidase multiplicity might be related to the observed differences in carbohydrate content, as suggested by recent reports on other microbial glycoprotein enzymes.
Mots-clé
Amino Acids/analysis, Aspergillus niger/*enzymology, Galactosidases/*metabolism, Glycoside Hydrolases/isolation & purification/metabolism, Isoenzymes/isolation & purification/*metabolism, Kinetics, Molecular Weight, Species Specificity, Substrate Specificity, beta-Galactosidase/isolation & purification/*metabolism
Pubmed
Création de la notice
13/08/2015 7:53
Dernière modification de la notice
20/08/2019 12:31
Données d'usage