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L-Galactose dehydrogenase

Laing, W.A., Fearson, N., Bulley, S., and MacRae, E., (2004), Kiwifruit L-galactose dehydrogenase Molecular, biochemical and physiological aspects of the enzyme. Fund. Plant Biol. 31 1015-1025. [Pg.41]

Figure 2. Enzymic measurement of a-L-arabinan in fruit-juice concentrates, (a) Effect of time of incubation of sample with arabinofuranosidase and ndo-arabinanase. Diluted pear juice concentrate (1 10 0.1 ml) or sugar beet arabinan solution (0.1 ml) was incubated with an aliquot (0.1 ml) of arabinofuranosidase (5 units) plus ndo-arabinanase (0.2 units) at 35 C and pH 4.0. Aliquots were analysed for arabinose. (b) Arabinose determination using the NAD-Galactose Dehydrogenase method. Arabinose solution (0.2 ml, 50 digrams) was incubated with Tris-HCl buffer (2.5 ml, pH 8.6), NAD (0.1 ml, 10 m ml) and galactose dehydrogenase (20/i, 140 milliunits) at 35°C. Absorbance (340 nm) was measured after various time intervals. Figure 2. Enzymic measurement of a-L-arabinan in fruit-juice concentrates, (a) Effect of time of incubation of sample with arabinofuranosidase and ndo-arabinanase. Diluted pear juice concentrate (1 10 0.1 ml) or sugar beet arabinan solution (0.1 ml) was incubated with an aliquot (0.1 ml) of arabinofuranosidase (5 units) plus ndo-arabinanase (0.2 units) at 35 C and pH 4.0. Aliquots were analysed for arabinose. (b) Arabinose determination using the NAD-Galactose Dehydrogenase method. Arabinose solution (0.2 ml, 50 digrams) was incubated with Tris-HCl buffer (2.5 ml, pH 8.6), NAD (0.1 ml, 10 m ml) and galactose dehydrogenase (20/i, 140 milliunits) at 35°C. Absorbance (340 nm) was measured after various time intervals.
Plants form ascorbate from GDP-mannose via GDP-L-galactose, L-galactose and L-galactono-1,4-lactone. The latter is oxidized to L-ascorbic acid by a mitochondrial L-galactono-1,4-lactone dehydrogenase, using cytochrome c as electron acceptor. The biosyntheis of L-ascorbic acid has been reviewed.337... [Pg.249]

Lindbladh, C., Persson, M., Bulow, L., and Mosbach, K. (1992). Characterization of a recombinant bifunctional enzyme, galactose dehydrogenase/bacterial luciferase,... [Pg.72]

An enzymic method which uses NAD-dependent L-fucose dehydrogenase can be used, in the absence of L-fucose to oxidize L-galactose liberated by hydrolysis of the polysaccharide.94... [Pg.22]

Enzymes, measured in clinical laboratories, for which kits are available include y-glutamyl transferase (GGT), alanine transferase [9000-86-6] (ALT), aldolase, a-amylase [9000-90-2] aspartate aminotransferase [9000-97-9], creatine kinase and its isoenzymes, galactose-l-phosphate uridyl transferase, Hpase, malate dehydrogenase [9001 -64-3], 5 -nucleotidase, phosphohexose isomerase, and pymvate kinase [9001-59-6]. One example is the measurement of aspartate aminotransferase, where the reaction is followed by monitoring the loss of NADH ... [Pg.40]

Ljungcrantz, P., Carlsson, H., Mansson, M. O., Buckel, P., Mosbach, K., and Bulow, L. (1989). Construction of an artificial bifunctional enzyme, beta-galactosidase/galac-tose dehydrogenase, exhibiting efficient galactose channeling. Biochemistry, 28,8786— 8792. [Pg.73]


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See also in sourсe #XX -- [ Pg.342 ]




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