Artículos de revistas
Production and characterization of Escherichia coli glycerol dehydrogenase as a tool for glycerol recycling
Fecha
2013-02Registro en:
Piattoni, Claudia Vanesa; Figueroa, Carlos Maria; Asención Diez, Matías Damián; Parcerisa, Ivana Lorna; Antuña, Sebastián; et al.; Production and characterization of Escherichia coli glycerol dehydrogenase as a tool for glycerol recycling; Elsevier; Process Biochemistry; 48; 3; 2-2013; 406-412
1359-5113
CONICET Digital
CONICET
Autor
Piattoni, Claudia Vanesa
Figueroa, Carlos Maria
Asención Diez, Matías Damián
Parcerisa, Ivana Lorna
Antuña, Sebastián
Comelli, Raul Alberto
Guerrero, Sergio Adrian
Beccaria, Alejandro José
Iglesias, Alberto Alvaro
Resumen
NAD+-dependent glycerol (Gro) dehydrogenase (GroDHase) catalyzes the conversion of Gro into dihydroxyacetone (DHA), the first step for fermentative Gro metabolism in Escherichia coli. In this work, we cloned the gldA gene that codes for the E. coli GroDHase and homologously expressed, purified, and kinetically characterized the recombinant protein. To achieve this, the enzyme was over-produced using Gro supplemented growth medium and lactose as the inducer. The enzyme was highly purified using either pseudo-affinity chromatography or a simple heat-shock treatment, which is potentially valuable for industrial production of GroDHase. We detected efficient oxidation of Gro derived from biodiesel production to DHA by gas chromatography. The results presented in this work support recombinant GroDHase production in a biorefinery setting as a relevant tool for converting Gro into DHA for future biotechnological applications.