- Email: [email protected]
Production of a bioemulsifier from a proprietary bacteria species for formation heavy oil–water emulsion
New Biotechnology · Volume 25S · September 2009
ABSTRACTS
2.1.089 Production of a bioemulsifier from a proprietary bacteria species for formation heavy oil—water emulsion A. Farahbakhsh 1,∗ , M. Taghizadeh 1 , B. Yakhchali 2 , K. Movagharnejad 1 1 College of Chemical Engineering, Babol Noshirvani University of Technology, Babol, Islamic Republic of Iran 2 National Institute of Genetic Engineering and Biotechnology (NIGEB), Tehran, Islamic Republic of Iran
(after 84 hours). Fourier transform infrared spectrum of extracted biosurfactant indicates the presence of carboxyl, amine, hydroxyl and methoxyl functional groups. Thermogram of biosurfactant demonstrated three sharp endothermic peaks placing between 200 and 280◦ C. The core holder flooding experiments demonstrated that the oil recovery efficiencies varied from 23.7 to 27.1% of residual oil. doi:10.1016/j.nbt.2009.06.337
2.1.091 Bioemulsifiers are a unique class of compounds that have a variety of potential applications in the use of bacteria, in enhanced oil recovery and reduce oil viscosity. In this project, a bioemulsifier was synthesized by strain of Bacillus licheniformis and was separated by autoclave and centrifugal process; the purification of bioemulsifier and the increase quality of product was done by add sulfuric acid (H2 SO4 ) (98%) to solution and centrifuged again. This bioemulsifier has the property of emulsification a wide range of heavy oils and crude oils to form a stable oil—water emulsion. doi:10.1016/j.nbt.2009.06.336
2.1.090 An efficient biosurfactant-producing bacterium Pseudomonas aeruginosa MR01, isolated from oil excavation areas in south of Iran T. Bagheri Lotfabad 1,∗ , F. Masoumi 2 , R. Roostaazad 1 , A. Saidi 3 , K. Akbari Noghabi 2 1
Department of Chemical and Petroleum Engineering, Sharif University of Technology, Tehran, Islamic Republic of Iran 2 National Institute of Genetic Engineering and Biotechnology (NIGEB), KarajTehran Highway, Pazhohesh Blvd, P.O. Box 14155-6343, Tehran, Iran 3 Department of Biotechnology, Faculty of New Technologies and Energy Engineering, Shahid Beheshti University, Evin, Tehran, Iran
A bacterial strain was isolated and cultured from the oil excavation areas in tropical zone in southern Iran. It was affiliated with Pseudomonas. The biochemical characteristics and partial sequenced 16S rRNA gene of isolate, MR01, was identical to those of cultured representatives of the species Pseudomonas aeruginosa. This bacterium was able to produce a type of biosurfactant with excessive foam-forming properties. Compositional analysis revealed that the extracted biosurfactant was composed of high percentages lipid (∼65%, w/w) and carbohydrate (∼30%, w/w) in addition to a minor fraction of protein (∼4%, w/w). The best production of 2.1 g/l was obtained when the cells were grown on minimal salt medium containing 1.2% (w/v) glucose and 0.1% (w/v) ammonium sulfate supplemented with 0.1% (w/v) isoleucine at 37◦ C and 180 rpm after two days. The optimum biosurfactant production pH value was found to be 8.0. The MR01 could reduce surface tension to 28 mN/m and emulsified hexadecane up to E24 70. The results obtained from time course study indicated that the surface tension reduction and emulsification potential was increased in the same way to cell growth. However, maximum biosurfactant production occurred and established in the stationary growth phase
S80
www.elsevier.com/locate/nbt
Purification and characterization of a novel aminopeptidase from solvent tolerant Pseudomonas aeruginosa PseA S. Khare ∗ , R. Gaur Institute of Technology Delhi, New Delhi, India
Aminopeptidases play an important role in industrial biocatalysis. They catalyze hydrolytic reactions under aqueous conditions and the reverse reaction in non-aqueous medium. The reverse reaction may be vitally useful in peptide/ester synthesis. To be used as biocatalysts for synthesis, aminopeptidases need to be stable in organic solvents. Present work describes an aminopeptidase from a solvent tolerant Pseudomonas aeruginosa PseA. The enzyme was purified to homogeneity by ion-exchange chromatography. Biochemical and molecular characterization place it among the zinc metallo-aminopeptidases. It exhibited Km of 3.02 mM and Vmax of 6.71 mol/mg/min towards L-leu-p-nitroanilide and found to be remarkably stable in wide range of organic solvents. Partial Nterminal sequence of purified enzyme showed exact match with P. aeruginosa PAO1 aminopeptidase coded by gene pepB. PCR amplified the 1611-bp open reading frame encoding a 57.51 kDa, 536 amino-acid protein. Analysis revealed the hydrophobic inclination of the protein. The 3D structure model of its M28 domain elucidated the presence of at least one S—S bridge. The striking solvent stability makes it a potential enzyme for application in non-aqueous system. doi:10.1016/j.nbt.2009.06.338
2.1.092 The crude oil degrading potential of Yarrowia lipolytica T. Ferreira 1,∗ , D. Azevedo 2 , M.A. Coelho 1 , M.H. Rocha-Leão 1 1
Departamento de Engenharia Bioquímica, Escola de Química, Universidade Federal do Rio de Janeiro, 21941-909, Brazil 2 Departamento de Química Orgânica, Instituto de Química, Universidade Federal do Rio de Janeiro, 21941-909, Brazil
Oil spills pose a great hazard for terrestrial and marine ecosystems. The total annual influx of oil into the sea is estimated to be approximately 5.2 million tones, and in productive areas it is almost unavoidable. Therefore, a search for new technologies to clean up oil-polluted environments is always welcome. Many microorganisms have the ability to utilize hydrocarbons as sole carbon sources
ABSTRACTS
2.1.089 Production of a bioemulsifier from a proprietary bacteria species for formation heavy oil—water emulsion A. Farahbakhsh 1,∗ , M. Taghizadeh 1 , B. Yakhchali 2 , K. Movagharnejad 1 1 College of Chemical Engineering, Babol Noshirvani University of Technology, Babol, Islamic Republic of Iran 2 National Institute of Genetic Engineering and Biotechnology (NIGEB), Tehran, Islamic Republic of Iran
(after 84 hours). Fourier transform infrared spectrum of extracted biosurfactant indicates the presence of carboxyl, amine, hydroxyl and methoxyl functional groups. Thermogram of biosurfactant demonstrated three sharp endothermic peaks placing between 200 and 280◦ C. The core holder flooding experiments demonstrated that the oil recovery efficiencies varied from 23.7 to 27.1% of residual oil. doi:10.1016/j.nbt.2009.06.337
2.1.091 Bioemulsifiers are a unique class of compounds that have a variety of potential applications in the use of bacteria, in enhanced oil recovery and reduce oil viscosity. In this project, a bioemulsifier was synthesized by strain of Bacillus licheniformis and was separated by autoclave and centrifugal process; the purification of bioemulsifier and the increase quality of product was done by add sulfuric acid (H2 SO4 ) (98%) to solution and centrifuged again. This bioemulsifier has the property of emulsification a wide range of heavy oils and crude oils to form a stable oil—water emulsion. doi:10.1016/j.nbt.2009.06.336
2.1.090 An efficient biosurfactant-producing bacterium Pseudomonas aeruginosa MR01, isolated from oil excavation areas in south of Iran T. Bagheri Lotfabad 1,∗ , F. Masoumi 2 , R. Roostaazad 1 , A. Saidi 3 , K. Akbari Noghabi 2 1
Department of Chemical and Petroleum Engineering, Sharif University of Technology, Tehran, Islamic Republic of Iran 2 National Institute of Genetic Engineering and Biotechnology (NIGEB), KarajTehran Highway, Pazhohesh Blvd, P.O. Box 14155-6343, Tehran, Iran 3 Department of Biotechnology, Faculty of New Technologies and Energy Engineering, Shahid Beheshti University, Evin, Tehran, Iran
A bacterial strain was isolated and cultured from the oil excavation areas in tropical zone in southern Iran. It was affiliated with Pseudomonas. The biochemical characteristics and partial sequenced 16S rRNA gene of isolate, MR01, was identical to those of cultured representatives of the species Pseudomonas aeruginosa. This bacterium was able to produce a type of biosurfactant with excessive foam-forming properties. Compositional analysis revealed that the extracted biosurfactant was composed of high percentages lipid (∼65%, w/w) and carbohydrate (∼30%, w/w) in addition to a minor fraction of protein (∼4%, w/w). The best production of 2.1 g/l was obtained when the cells were grown on minimal salt medium containing 1.2% (w/v) glucose and 0.1% (w/v) ammonium sulfate supplemented with 0.1% (w/v) isoleucine at 37◦ C and 180 rpm after two days. The optimum biosurfactant production pH value was found to be 8.0. The MR01 could reduce surface tension to 28 mN/m and emulsified hexadecane up to E24 70. The results obtained from time course study indicated that the surface tension reduction and emulsification potential was increased in the same way to cell growth. However, maximum biosurfactant production occurred and established in the stationary growth phase
S80
www.elsevier.com/locate/nbt
Purification and characterization of a novel aminopeptidase from solvent tolerant Pseudomonas aeruginosa PseA S. Khare ∗ , R. Gaur Institute of Technology Delhi, New Delhi, India
Aminopeptidases play an important role in industrial biocatalysis. They catalyze hydrolytic reactions under aqueous conditions and the reverse reaction in non-aqueous medium. The reverse reaction may be vitally useful in peptide/ester synthesis. To be used as biocatalysts for synthesis, aminopeptidases need to be stable in organic solvents. Present work describes an aminopeptidase from a solvent tolerant Pseudomonas aeruginosa PseA. The enzyme was purified to homogeneity by ion-exchange chromatography. Biochemical and molecular characterization place it among the zinc metallo-aminopeptidases. It exhibited Km of 3.02 mM and Vmax of 6.71 mol/mg/min towards L-leu-p-nitroanilide and found to be remarkably stable in wide range of organic solvents. Partial Nterminal sequence of purified enzyme showed exact match with P. aeruginosa PAO1 aminopeptidase coded by gene pepB. PCR amplified the 1611-bp open reading frame encoding a 57.51 kDa, 536 amino-acid protein. Analysis revealed the hydrophobic inclination of the protein. The 3D structure model of its M28 domain elucidated the presence of at least one S—S bridge. The striking solvent stability makes it a potential enzyme for application in non-aqueous system. doi:10.1016/j.nbt.2009.06.338
2.1.092 The crude oil degrading potential of Yarrowia lipolytica T. Ferreira 1,∗ , D. Azevedo 2 , M.A. Coelho 1 , M.H. Rocha-Leão 1 1
Departamento de Engenharia Bioquímica, Escola de Química, Universidade Federal do Rio de Janeiro, 21941-909, Brazil 2 Departamento de Química Orgânica, Instituto de Química, Universidade Federal do Rio de Janeiro, 21941-909, Brazil
Oil spills pose a great hazard for terrestrial and marine ecosystems. The total annual influx of oil into the sea is estimated to be approximately 5.2 million tones, and in productive areas it is almost unavoidable. Therefore, a search for new technologies to clean up oil-polluted environments is always welcome. Many microorganisms have the ability to utilize hydrocarbons as sole carbon sources