- Email: [email protected]
Comparative analysis of protein pattern of Sinorhizobium meliloti isolates
S252
Abstracts
biochemical properties and behavior. It can be concluded that the PPO enzyme prepared from F. carica possesses diphenolase activity, having the greatest substrate specificity to 4-methylpyrocatecol. The enzyme appears to share some biochemical characteristics of several plant PPOs in terms of substrate specificity, pH and temperature optima and stability. In addition, the enzyme activity was very sensitive to some general PPO inhibitors, especially ascorbic acid and l-cysteine. Keywords: Polyphenol oxidase, Kinetics, Thermal stability doi:10.1016/j.clinbiochem.2011.08.625
E.poster – [A-10-1221-2] Comparative analysis of protein pattern of Sinorhizobium meliloti isolates Mahboobeh Nakhaei Moghaddam, Zahra Mortezaei Department of Biology, Mashhad Branch, Islamic Azad University, Mashhad, Iran E-mail address: [email protected] (M. Nakhaei Moghaddam) Introduction: Sinorhizobium meliloti is a bacterium that biologically fix nitrogen and improve the growth of alfalfa (Medicago sativa) plants. In this study, native coexisting rhizobia were isolated from alfalfa plants and their protein patterns were compared. Methods: Healthy plants with roots were collected from Khorasan provinces, including Ferdowsi road, Bojnurd, cis-Abad, Faizabad and Shandiz, in late March and April 2009. Alfalfa plants were confirmed by experts. Nodules were disinfected and suspension of them were cultured on specific medium. Suspected bacteria were identified using Gram staining, catalase and oxidase tests. Isolated bacteria were tested for some biochemical reactions. The total protein patterns of isolates were compared using SDS-PAGE. Results: Protein patterns of two isolates, No. 06 and 09, had more similarities, but in overall the isolates had different protein patterns. Discussion: Protein patterns of two isolates, No. 06 and 09, had more similarities, but in overall the isolates had different protein patterns. Keywords: Sinorhizobium meliloti, Protein pattern, Alfalfa doi:10.1016/j.clinbiochem.2011.08.626
Poster – [A-10-1261-1] The effect of crude oil and hexadecane on the activity of alkaline phosphatase of Pseudomonas aeruginosa Hadise Sangsefidi, Dariush Minaee-Tehrani, Fereshte Eftekhar Tehran -Evin- Shahid Beheshti University, Iran E-mail addresses: [email protected] (H. Sangsefidi), [email protected] (D. Minaee-Tehrani), [email protected] (F. Eftekhar) Introduction: Pseudomonas belongs to the category of gramnegative bacteria and is useful for biodegradation of organic pollutant such as crude oil in soil. This bacterium can use crude oil or its by products as the only carbon source and change them to nontoxic materials. Alkaline phosphatase is an enzyme with a broad range of substrates and is responsible in removing phosphate group from substrate in alkaline condition. In the present work the effect of light crude oil and its by product, hexadecane, on the activity of alkaline phosphatase of Pseudomonas was studied and compared with the media containing glucose and ethanol. Results: Our results showed that in all the media the activity of enzyme reached maximum in the early stationary phase. In glucose
and ethanol containing media, the growth curve of bacterium reached stationary phase after 74 h while in both crude oil and hexadecane the stationary phase started after 190 h. In all the media the optimum enzyme activity was observed at pH = 7 and 40 °C. The specific enzyme activity was measured to be 0.5 × 10− 6 in ethanol, 0.07 × 10− 6 for glucose, 0.1 × 10− 6 for hexadecane and 0.09 × 10− 6 U/ mg protein for crude oil. The highest biomass was observed on hexadecane (4.8 g/L) while the lowest was seen in glucose (1.5 g/L). Conclusion: Our results showed that the activity and kinetics parameters (Km and Vmax) of enzyme have been changed in different carbon sources which suggest that the bacterium may use various isoforms of enzyme in different carbon sources. Keywords: Alkaline phosphatase, Enzyme, Pseudomonas, Crude oil doi:10.1016/j.clinbiochem.2011.08.627
Poster – [A-10-1262-1] Change of peroxidase activity of lentil (Lens culinaris) in the presence of light crude oil in soil Narjes Naemia, Dariush Minaee-Tehranib, Behzad Laameh-Radc a Payam noor University, Tehran, Iran b Tehran -Evin- Shahid Beheshti University, Iran c Tehran Ferdowsi Square, Iran E-mail addresses: [email protected] (N. Naemi), [email protected] (D. Minaee-Tehrani), [email protected] (B. Laameh-Rad) Introduction: Peroxidases are a group of enzymes that catalyze oxidation–reduction reactions. This group of enzymes occurs especially in plant cells, and catalyzes the oxidation of a substance by peroxide. The spillage of crude oil in to the soil causes damages to the environment and changes the biological and physicochemical properties of the soil. Some petroleum components are toxic for living organisms, however, some plants and microorganisms are able to biodegrade the crude oil hydrocarbons into products less toxic than the parent compounds. The presence of oil in the soil may cause some morphological, enzymatic changes in plants. In this study the effect of light crude oil on the activity of peroxidase of lentil was studied. Results: Our results showed that the activity of enzyme in the root increased in the presence of crude oil (3.14 U/mg protein) in comparison with the shoots (1.02 U/protein) while the activity of enzyme was nearly the same in the root (4.28 U/mg protein) and shoots (5.28 U/mg protein) of the control sample. The Km of enzyme was increased in the root of contaminated sample (16.6 mM) in comparison with the control (10 mM). However the Km of the shoot decreased in contaminated sample (3.3 mM) in comparison with the control (10 mM). Conclusion: In conclusion, there was a significant change of root peroxidase activity in contaminated sample which proposed that an isoform of peroxidase enzyme has been produced in contaminated root which was in direct contact with crude oil.
Keywords: Lentil, Crude oil, Peroxidase, Enzyme, Contamination doi:10.1016/j.clinbiochem.2011.08.628
Oral – [A-10-1295-1] Epac, not PKA, mediate the antiproliferative effects of cyclic AMP on human arteriolar smooth muscle cells Hussein Eid Ali Qatar University, Qatar
Abstracts
biochemical properties and behavior. It can be concluded that the PPO enzyme prepared from F. carica possesses diphenolase activity, having the greatest substrate specificity to 4-methylpyrocatecol. The enzyme appears to share some biochemical characteristics of several plant PPOs in terms of substrate specificity, pH and temperature optima and stability. In addition, the enzyme activity was very sensitive to some general PPO inhibitors, especially ascorbic acid and l-cysteine. Keywords: Polyphenol oxidase, Kinetics, Thermal stability doi:10.1016/j.clinbiochem.2011.08.625
E.poster – [A-10-1221-2] Comparative analysis of protein pattern of Sinorhizobium meliloti isolates Mahboobeh Nakhaei Moghaddam, Zahra Mortezaei Department of Biology, Mashhad Branch, Islamic Azad University, Mashhad, Iran E-mail address: [email protected] (M. Nakhaei Moghaddam) Introduction: Sinorhizobium meliloti is a bacterium that biologically fix nitrogen and improve the growth of alfalfa (Medicago sativa) plants. In this study, native coexisting rhizobia were isolated from alfalfa plants and their protein patterns were compared. Methods: Healthy plants with roots were collected from Khorasan provinces, including Ferdowsi road, Bojnurd, cis-Abad, Faizabad and Shandiz, in late March and April 2009. Alfalfa plants were confirmed by experts. Nodules were disinfected and suspension of them were cultured on specific medium. Suspected bacteria were identified using Gram staining, catalase and oxidase tests. Isolated bacteria were tested for some biochemical reactions. The total protein patterns of isolates were compared using SDS-PAGE. Results: Protein patterns of two isolates, No. 06 and 09, had more similarities, but in overall the isolates had different protein patterns. Discussion: Protein patterns of two isolates, No. 06 and 09, had more similarities, but in overall the isolates had different protein patterns. Keywords: Sinorhizobium meliloti, Protein pattern, Alfalfa doi:10.1016/j.clinbiochem.2011.08.626
Poster – [A-10-1261-1] The effect of crude oil and hexadecane on the activity of alkaline phosphatase of Pseudomonas aeruginosa Hadise Sangsefidi, Dariush Minaee-Tehrani, Fereshte Eftekhar Tehran -Evin- Shahid Beheshti University, Iran E-mail addresses: [email protected] (H. Sangsefidi), [email protected] (D. Minaee-Tehrani), [email protected] (F. Eftekhar) Introduction: Pseudomonas belongs to the category of gramnegative bacteria and is useful for biodegradation of organic pollutant such as crude oil in soil. This bacterium can use crude oil or its by products as the only carbon source and change them to nontoxic materials. Alkaline phosphatase is an enzyme with a broad range of substrates and is responsible in removing phosphate group from substrate in alkaline condition. In the present work the effect of light crude oil and its by product, hexadecane, on the activity of alkaline phosphatase of Pseudomonas was studied and compared with the media containing glucose and ethanol. Results: Our results showed that in all the media the activity of enzyme reached maximum in the early stationary phase. In glucose
and ethanol containing media, the growth curve of bacterium reached stationary phase after 74 h while in both crude oil and hexadecane the stationary phase started after 190 h. In all the media the optimum enzyme activity was observed at pH = 7 and 40 °C. The specific enzyme activity was measured to be 0.5 × 10− 6 in ethanol, 0.07 × 10− 6 for glucose, 0.1 × 10− 6 for hexadecane and 0.09 × 10− 6 U/ mg protein for crude oil. The highest biomass was observed on hexadecane (4.8 g/L) while the lowest was seen in glucose (1.5 g/L). Conclusion: Our results showed that the activity and kinetics parameters (Km and Vmax) of enzyme have been changed in different carbon sources which suggest that the bacterium may use various isoforms of enzyme in different carbon sources. Keywords: Alkaline phosphatase, Enzyme, Pseudomonas, Crude oil doi:10.1016/j.clinbiochem.2011.08.627
Poster – [A-10-1262-1] Change of peroxidase activity of lentil (Lens culinaris) in the presence of light crude oil in soil Narjes Naemia, Dariush Minaee-Tehranib, Behzad Laameh-Radc a Payam noor University, Tehran, Iran b Tehran -Evin- Shahid Beheshti University, Iran c Tehran Ferdowsi Square, Iran E-mail addresses: [email protected] (N. Naemi), [email protected] (D. Minaee-Tehrani), [email protected] (B. Laameh-Rad) Introduction: Peroxidases are a group of enzymes that catalyze oxidation–reduction reactions. This group of enzymes occurs especially in plant cells, and catalyzes the oxidation of a substance by peroxide. The spillage of crude oil in to the soil causes damages to the environment and changes the biological and physicochemical properties of the soil. Some petroleum components are toxic for living organisms, however, some plants and microorganisms are able to biodegrade the crude oil hydrocarbons into products less toxic than the parent compounds. The presence of oil in the soil may cause some morphological, enzymatic changes in plants. In this study the effect of light crude oil on the activity of peroxidase of lentil was studied. Results: Our results showed that the activity of enzyme in the root increased in the presence of crude oil (3.14 U/mg protein) in comparison with the shoots (1.02 U/protein) while the activity of enzyme was nearly the same in the root (4.28 U/mg protein) and shoots (5.28 U/mg protein) of the control sample. The Km of enzyme was increased in the root of contaminated sample (16.6 mM) in comparison with the control (10 mM). However the Km of the shoot decreased in contaminated sample (3.3 mM) in comparison with the control (10 mM). Conclusion: In conclusion, there was a significant change of root peroxidase activity in contaminated sample which proposed that an isoform of peroxidase enzyme has been produced in contaminated root which was in direct contact with crude oil.
Keywords: Lentil, Crude oil, Peroxidase, Enzyme, Contamination doi:10.1016/j.clinbiochem.2011.08.628
Oral – [A-10-1295-1] Epac, not PKA, mediate the antiproliferative effects of cyclic AMP on human arteriolar smooth muscle cells Hussein Eid Ali Qatar University, Qatar