2,000 Units at 40oC
Prices exclude VAT
Available for shipping
|Content:||2,000 Units at 40oC|
|Formulation:||In 3.2 M ammonium sulphate|
|Stability:||Minimum 1 year at 4oC. Check vial for details.|
|Concentration:||Supplied at ~ 1,000 U/mL|
|Expression:||Recombinant from Penicillium simplicissimum|
|Specificity:||Hydrolysis of terminal, non-reducing α-D-galactose residues in α-D-galactosides, including galacto-oligosaccharides and galactomannans.|
|Specific Activity:||~ 160 U/mg (40oC, pH 3.5 on p-nitrophenyl-α-D-galactopyranoside)|
|Unit Definition:||One Unit of α-galactosidase activity is defined as the amount of enzyme required to release one µmole of of p-nitrophenol per minute from p-nitrophenyl-α-D-galactopyranoside (5 mM) in glycine buffer (100 mM), pH 3.5 at 40oC.|
|Application examples:||For use in glycobiology, carbohydrate or biofuels research.|
High purity α-Galactosidase (Penicillium simplicissimum) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.
View all CAZy enzyme products available.
McCleary, B. V. & Matheson, N. K. (1974). Phytochemistry, 13(9), 1747-1757.
Germinating seeds of lucerne, guar, carob and soybean initially depleted raffinose series oligosaccharides and then galactomannan. This depletion was accompanied by a rapid increase and then a decrease in α-galactosidase levels. Lucerne and guar contained two α-galactosidase activities, carob three and soybean four. One of these in each plant, from its location in the endosperm, time of appearance and kinetic behaviour, appeared to be primarily involved in galactomannan hydrolysis. This enzyme in lucerne had MW of 23 000 and could not be separated from β-mannanase by (NH4)2SO4 fractionation, DEAE, CM or SE-cellulose chromatography or gel filtration, but only by polyacrylamide gel electrophoresis. In guar, carob and soybean, it could be separated by ion-exchange chromatography and gel filtration. In lucerne, carob and guar most of the total increase in activity was due to this enzyme. The other α-galactosidases had MWs of about 35 000 and could be separated from β-mannanase by dissection, ion exchange cellulose chromatography and gel filtration. They were located in the cotyledon-embryo and appeared to be primarily involved in galactosylsucrose oligosaccharide hydrolysis.Hide Abstract