Purification and molecular properties of an alpha-galactosidase synthesized and secreted by Aspergillus nidulans

alpha-Galactosidases from mycelial extract and culture filtrate of Aspergillus nidulans have been purified to homogeneity and utilised to obtain polyclonal antibodies anti-alpha-galactosidase. The enzymatic characteristics and the cross reactivity of the antibodies suggest that alpha-galactosidases...

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Bibliographic Details
Published in:FEMS microbiology letters 1993-08, Vol.112 (1), p.35-41
Main Authors: Rios, S, Pedregosa, A.M, Monistrol, I.F, Laborda, F
Format: Article
Language:English
Subjects:
alpha-galactosidase
alpha-Galactosidase - biosynthesis
alpha-Galactosidase - chemistry
alpha-Galactosidase - isolation & purification
Aspergillus nidulans
Aspergillus nidulans - enzymology
Aspergillus nidulellus
Biological and medical sciences
culture filtrates
culture media
Enzyme Stability
Fundamental and applied biological sciences. Psychology
Growth, nutrition, metabolism, transports, enzymes. Molecular biology
Hydrogen-Ion Concentration
Immunochemistry
Microbiology
Molecular Weight
mycelium
Mycology
physicochemical properties
plant extracts
Protein Conformation
protein secretion
protein synthesis
purification
Temperature
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Summary:alpha-Galactosidases from mycelial extract and culture filtrate of Aspergillus nidulans have been purified to homogeneity and utilised to obtain polyclonal antibodies anti-alpha-galactosidase. The enzymatic characteristics and the cross reactivity of the antibodies suggest that alpha-galactosidases isolated from the two sources were the same enzyme. Thus, A. nidulans synthesized and secreted only one enzymatic form of alpha-galactosidase which is a multimeric enzyme of 370 kDa composed of four monomers of 87 kDa and a pl of 6.3. The optimum temperature of activity was 50 degrees C and the optimum pH 4-5. The enzyme was stable over a wide range of pH but quite unstable to temperature. alpha-Galactosidase of A. nidulans is a very specific enzyme, it is active only on p-nitrophenyl-alpha-D-galactoside (PNPG), melibiose and raffinose. When PNPG was utilised as substract melibiose, raffinose, galactose and glucose were competitive inhibitors of the activity.
ISSN:0378-1097
1574-6968
DOI:10.1016/0378-1097(93)90534-9