José Eduardo Arteaga1, Karina Cerros1, Ernesto Rivera-Becerril2, Alvaro R Lara3, Sylvie Le Borgne3, Juan-Carlos Sigala4. 1. Posgrado en Ciencias Naturales e Ingeniería, Universidad Autónoma Metropolitana, Unidad Cuajimalpa, 05348, Mexico City, Mexico. 2. Departamento de Ciencias Naturales, Universidad Autónoma Metropolitana, Unidad Cuajimalpa, 05348, Mexico City, Mexico. 3. Departamento de Procesos y Tecnología, Universidad Autónoma Metropolitana, Unidad Cuajimalpa. Av. Vasco de Quiroga 4871, Col. Santa Fe Cuajimalpa, Alcaldía Cuajimalpa, 05348, Mexico City, Mexico. 4. Departamento de Procesos y Tecnología, Universidad Autónoma Metropolitana, Unidad Cuajimalpa. Av. Vasco de Quiroga 4871, Col. Santa Fe Cuajimalpa, Alcaldía Cuajimalpa, 05348, Mexico City, Mexico. jsigala@cua.uam.mx.
Abstract
OBJECTIVES: To determine furfural biotransformation capabilities of Acinetobacter baylyi ADP1 and Acinetobacter schindleri ACE. RESULTS: Acinetobacter baylyi ADP1 and A. schindleri ACE could not use furfural as sole carbon source but when acetate was used as substrate, ADP1 and ACE biotransformed 1 g furfural/l in 5 and 9 h, respectively. In both cases, the product of this biotransformation was difurfuryl-ether as shown by FT-IR and 1H and 13C NMR spectroscopy. The presence of furfural decreased the specific growth rate in acetate by 27% in ADP1 and 53% in ACE. For both strains, the MIC of furfural was 1.25 g/l. Nonetheless, ADP1 biotransformed 2 g furfural/l at a rate of 1 g/l/h in the stationary phase of growth. A transcriptional analysis of possible dehydrogenases involved in this biotransformation, identified that the areB and frmA genes were highly overexpressed after the exposure of ADP1 to furfural. The products of these genes are a benzyl-alcohol dehydrogenase and an alcohol dehydrogenase. CONCLUSIONS: Acinetobacter baylyi ADP1 is a candidate for the biological detoxification of furfural, a fermentation inhibitor present in lignocellulosic hydrolysates, with the possible direct involvement of the AreB and FrmA enzymes in the process.
OBJECTIVES: To determine furfural biotransformation capabilities of Acinetobacter baylyi ADP1 and Acinetobacter schindleri ACE. RESULTS:Acinetobacter baylyi ADP1 and A. schindleri ACE could not use furfural as sole carbon source but when acetate was used as substrate, ADP1 and ACE biotransformed 1 g furfural/l in 5 and 9 h, respectively. In both cases, the product of this biotransformation was difurfuryl-ether as shown by FT-IR and 1H and 13C NMR spectroscopy. The presence of furfural decreased the specific growth rate in acetate by 27% in ADP1 and 53% in ACE. For both strains, the MIC of furfural was 1.25 g/l. Nonetheless, ADP1 biotransformed 2 g furfural/l at a rate of 1 g/l/h in the stationary phase of growth. A transcriptional analysis of possible dehydrogenases involved in this biotransformation, identified that the areB and frmA genes were highly overexpressed after the exposure of ADP1 to furfural. The products of these genes are a benzyl-alcohol dehydrogenase and an alcohol dehydrogenase. CONCLUSIONS:Acinetobacter baylyi ADP1 is a candidate for the biological detoxification of furfural, a fermentation inhibitor present in lignocellulosic hydrolysates, with the possible direct involvement of the AreB and FrmA enzymes in the process.
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