SciELO - Scientific Electronic Library Online

vol.57 número1Catalytic Properties of Pure and K+-Doped CuO/MgO System Towards 2-Propanol ConversionBehavior of Two and Three Electrode Configuration and Different Mediators in Working Electrode on Development of Disposable Screen-Printing Biosensors for Determination of Free Cholesterol índice de autoresíndice de materiabúsqueda de artículos
Home Pagelista alfabética de revistas  

Servicios Personalizados




Links relacionados

  • No hay artículos similaresSimilares en SciELO


Journal of the Mexican Chemical Society

versión impresa ISSN 1870-249X


LUNA, Héctor et al. Comparative Study on the N-acylase Activity of Mammalian Kidney Acetone Powders (KAP's). J. Mex. Chem. Soc [online]. 2013, vol.57, n.1, pp.43-46. ISSN 1870-249X.

The N-acylase activity and enantioselectivity of mammalian kidney acetone powders (KAP's) or their enzyme extract was demonstrated on (rac)-N-acetylmethionine; used as reference substrate. It was showed hydrolysis exclusively on the (S)-enantiomer. The biocatalyzed reaction allowed us, to categorize the KAPs regarding the animal source, sheep, pig, calf, bovine, dog and guinea pig as fast biocatalysts reaching equilibrium in around 4 to 5 h; and rat, mouse and hamster were slower biocatalysts, since they did it in around 24 h. In most of the reactions the kidney crude preparations gave a better conversion than the enzyme extract, this fact demonstrated that the longer stirring during the reaction in an aqueous medium, allowed a greater dissolution of the enzyme. These readily available and inexpensive crude biocatalysts have a great potential application in organic synthesis.

Palabras llave : Kidney Acetone Poder; Acylase; Enzymatic Resolution; Amino Acids; Deacylation.

        · resumen en Español     · texto en Inglés     · Inglés ( pdf )


Creative Commons License Todo el contenido de esta revista, excepto dónde está identificado, está bajo una Licencia Creative Commons