The development of an immobilized enzyme reactor containing glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzi: the effect of species' specific differences on the immobilization

Literature Information

Publication Date 2007-10-08
DOI 10.1039/B711145B
Impact Factor 4.616
Authors

Carmen Lúcia Cardoso, Marcela Cristina de Moraes, Rafael Victorio Carvalho Guido, Glaucius Oliva, Adriano Defini Andricopulo, Irving William Wainer, Quezia Bezerra Cass


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Abstract

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in the life cycle of the Trypanosoma cruzi, and an immobilized enzyme reactor (IMER) has been developed for use in the on-line screening for GAPDH inhibitors. An IMER containing human GAPDH has been previously reported; however, these conditions produced a T. cruzi GAPDH-IMER with poor activity and stability. The factors affecting the stability of the human and T. cruzi GAPDHs in the immobilization process and the influence of pH and buffer type on the stability and activity of the IMERs have been investigated. The resulting T. cruzi GAPDH-IMER was coupled to an analytical octyl column, which was used to achieve chromatographic separation of NAD+ from NADH. The production of NADH stimulated by D-glyceraldehyde-3-phosphate was used to investigate the activity and kinetic parameters of the immobilized T. cruzi GAPDH. The Michaelis–Menten constant (Km) values determined for D-glyceraldehyde-3-phosphate and NAD+ were Km = 0.5 ± 0.05 mM and 0.648 ± 0.08 mM, respectively, which were consistent with the values obtained using the non-immobilized enzyme.

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