Production and Characterization of Escherichia coli Glycerol Dehydrogenase as a Tool for Glycerol Recycling

C.V. PIATTONI; C.M. FIGUEROA; M.D. ASENCIÓN DIEZ; I.L. PARCERISA; S. ACUÑA; R.A. COMELLI; S.A. GUERRERO; A.A. IGLESIAS

PROCESS BIOCHEMISTRY - (Print)

ELSEVIER SCI LTD

Lugar: Amsterdam; Año: 2013 vol. 48 p. 406 - 412

1359-5113

NAD+-dependent glycerol (Gro) dehydrogenase (GroDHase) catalyzes the conversion of Gro into dihydroxyacetone  (DHA),  the  first  step  for  fermentative  Gro  metabolism  in  Escherichia  coli. 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  valuable for  industrial production of GroDHase. We detected efficient oxidation of Gro derived from biodieselproduction  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.