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http://dx.doi.org/10.3746/jfn.2009.14.4.358

Purification of Aldose Reductase and Decolorization of Dye by the Enzyme  

Jang, Mi (Department of Chemistry, Myongji University)
Kim, Kyung-Soon (Department of Chemistry, Myongji University)
Publication Information
Preventive Nutrition and Food Science / v.14, no.4, 2009 , pp. 358-361 More about this Journal
Abstract
Aldose reductase was purified to electrophoretic homogeneity from porcine liver. The purified enzyme was a monomer of 36 kDa. The enzyme was strongly inhibited by $Cu^{2+}\;and\;Mg^{2+}$ ions. Incubation of the enzyme with pyridoxal 5'-phosphate led to complete inhibition of enzymatic activity, suggesting that lysine residue is involved at or near the active site of the enzyme. The enzyme exhibited a broad substrate specificity. Furthermore, the enzyme was capable of decolorizing Alizarin, an anthraquinone dye.
Keywords
aldose reductase; purification; property; color removal;
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