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Omidinia, E.. (1390). Production of Recombinant Proline Dehydrogenase Enzyme from Pseudomonas fluorescens pf-5 in E. coli System. , 22(4), 321-327.
E. Omidinia. "Production of Recombinant Proline Dehydrogenase Enzyme from Pseudomonas fluorescens pf-5 in E. coli System". , 22, 4, 1390, 321-327.
Omidinia, E.. (1390). 'Production of Recombinant Proline Dehydrogenase Enzyme from Pseudomonas fluorescens pf-5 in E. coli System', , 22(4), pp. 321-327.
Omidinia, E.. Production of Recombinant Proline Dehydrogenase Enzyme from Pseudomonas fluorescens pf-5 in E. coli System. , 1390; 22(4): 321-327.

Production of Recombinant Proline Dehydrogenase Enzyme from Pseudomonas fluorescens pf-5 in E. coli System

Journal of Sciences, Islamic Republic of Iran
مقاله 3، دوره 22، شماره 4، اسفند 2011، صفحه 321-327    اصل مقاله (265.65 K)
نویسنده
E. Omidinia
Pasteur Institute of Iran
چکیده
Proline dehydrogenase (ProDH; 1.5.99.8) belongs to superfamily of amino acid dehydrogenase, which plays a significant role in the metabolic pathway from proline to glutamate. The goal of this research was gene cloning and characterization of ProDH enzyme from Pseudomonas fluorescens pf-5 strain. The gene encoding ProDH was isolated by means of PCR amplification and cloned in an IPTG inducible T7-based expression system. The Histidine-tagged recombinant enzyme was purified and its kinetic properties were studied. According to SDS-PAGE analysis ProDH revealed a MW of 40 kDa. The Km and Vmax values of P. fluorescens ProDH were estimated to be 20 mM and 160 ?mol/min, respectively. ProDH activity was stable at alkaline pH and the highest activity was observed at pH 8.5 and 30°C. This study is the first data on the isolation and production of P. fluorescens ProDH enzyme in E. coli expression system.
کلیدواژه‌ها
Cloning؛ pseudomonas fluorescence؛ Characterization؛ Proline dehydrogenase (ProDH)
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