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- W2477121713 abstract "D-Galactonate dehydratase (EC 4.2.1.6) and 2-keto-3-deoxy-D-galactonate (KDGal) aldolase (lyase division; similar to EC 4.1.2.21, but without phosphorolytic reaction) were purified from cell-free extracts of Aspergillus niger by ion exchange column chromatography using diethylaminoethyl (DEAE)-cellulose. The highest specific activity was found in fraction numbers 35 and 28 corresponding to a 30 and 73-fold purification for these two enzymes, respectively. Some properties of the purified KDGal aldolase were studied. The enzyme exhibited the optimum pH and temperature at 7.5 and 50 °C, respectively. Potassium phosphate buffer showed the highest KDGal aldolase activity when compared to the analogous activity obtained with the other buffers used. The results also indicated that the catalytic activity of the purified enzyme was proportional to the amount of protein in question and a linear relationship was obtained. The effect of the concentrations of the three substrates namely KDGal, pyruvate and glyceraldehyde on the activity of KDGal aldolase was studied. From a Lineweaver-Burk plot of the reciprocal of initial velocities and substrate concentrations the Km (Michaelis constant) values were calculated and found to be 7.69, 12.20 and 6.25 mM, respectively, indicating the highest affinity of the enzyme for glyceraldehyde." @default.
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- W2477121713 date "2002-06-27" @default.
- W2477121713 modified "2023-09-23" @default.
- W2477121713 title "Purification and enzymic properties of KDGal aldolase from Aspergillus niger" @default.
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