Enzyme Activity Measurement for D-iditol 2-dehydrogenase Using Spectrophotometric Assays

Creative Enzymes’ leading position in activity measurement is marked deeply by customized services, such as activity assays for D-iditol 2-dehydrogenases by spectrophotometric assays. Actually, little studies focused on this enzyme is the most common inner obstacle in the way of industrialization of its activity measurement. However, with the advanced equipment and experienced scientists, Creative Enzymes is able to perform precise and fast activity assays for D-iditol 2-dehydrogenases.

D-iditol 2-dehydrogenases (EC 1.1.1.15) is a member of oxidoreductases, more precisely, the oxidoreductases that act on the CH-OH group of the electron donor with NAD+ (nicotinamide adenine dinucleotide) or NADP+ (nicotinamide adenine dinucleotide phosphate) as the electron acceptor. This enzyme mainly catalyzes two substrates, D-iditol and NAD+, to three products, D-sorbose, NADH and proton. The enzymatic activities that convert xylitol into L-xylulose and L-glucitol into L-fructose were also reported. The systematic name of this enzyme class is D-iditol: NAD+ 2-oxidoreductase, and it was also named as D-sorbitol dehydrogenase.

The enzyme, together with some other enzymes, can interconvert D-Sorbitol and D-Fructose, which is involved in fructose and mannose metabolism. It is widely known that fructose, a simple ketone sugar, is one of the three dietary monosaccharides, along with glucose and galactose. The three monosaccharides are absorbed directly into the bloodstream during digestion and later metabolized to provide energy to biological activities. Whereas mannose, a C-2 epimer of glucose, is important in human metabolism including the glycosylation of certain proteins. Therefore, D-iditol 2-dehydrogenase is an essential enzyme in both energy production and function regulations. In addition, the enzyme can participate in transferring xylitol into L-xylulose in pentose and glucuronate interconversions. In many ways, the significance of D-iditol 2-dehydrogenases attracted fast-growing attentions of many industries. Nonetheless, lack of detailed understanding of the biophysics and biochemistry of the enzyme prevents most researchers from activity quantification.

Creative Enzymes is able to provide activity measurement for D-iditol 2-dehydrogenases to promote specific studies related to the development and utilization of the enzyme. In addition, our better understanding of the properties of D-iditol 2-dehydrogenases also enables us to keep improving the current activity measurement.

Figure: Molecule diagrams of the chemical reaction catalyzed by D-iditol 2-dehydrogenases: D-Iditol + NAD+ => D-Sorbose + NADH + H+.