Proceedings of the Plant Resources Society of Korea Conference (한국자원식물학회:학술대회논문집)
- 2010.05a
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- Pages.17-17
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- 2010
Enzymatic characterization and Expression of 1-aminocycloprophane-1-carboxlyate deaminase from the rhizobacterium Pseudomonas flourescens
- Lee, Gun-Woong (Division of Biotechnology, College of Environmental & Bioresource Sciences, Chonbuk National University) ;
- Ju, Jae-Eun (Division of Biotechnology, College of Environmental & Bioresource Sciences, Chonbuk National University) ;
- Kim, Hae-Min (Division of Biotechnology, College of Environmental & Bioresource Sciences, Chonbuk National University) ;
- Lee, Si-Nae (Division of Biotechnology, College of Environmental & Bioresource Sciences, Chonbuk National University) ;
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Chae, Jong-Chan
(Division of Biotechnology, College of Environmental & Bioresource Sciences, Chonbuk National University) ;
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Lee, Yong-Hoon
(Division of Biotechnology, College of Environmental & Bioresource Sciences, Chonbuk National University) ;
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Oh, Byung-Taek
(Division of Biotechnology, College of Environmental & Bioresource Sciences, Chonbuk National University) ;
- Soh, Byoung-Yul (Division of Biotechnology, College of Environmental & Bioresource Sciences, Chonbuk National University)
- Published : 2010.05.14
Abstract
Ethylene, known as a stress hormone regulate wide developmental processes including germination, root hair initiation, root and shoot primordial formation and elongation, leaf and flower senescence and abscission, fruit ripening. The acceleration of ethylene biosynthesis in plant associated with environmental and biological stresses. 1-Aminocycloprophane-1-carboxlyate deaminase(ACCD) is an enzyme that cleaves ACC into and ammonia, a precursor of the plant hormone ethylene. Plant growth-promoting rhizobacteria (PGPR) having ACCD can decrease endogenous ACC level of tissue, resulting in reduced production of ethylene in plants. ACC deaminse was a key enzyme for protect stressed plants from injurious effects of ethylene. ACCD gene was encoded from Pseudomonas flourescens, PGPR and was cloned in Escherichia coli. We expressed the recombinant ACCD(rACCD) containing 357 amino acids with molecular weight 39 kDa that revealed by SDS-PAGE and western blot. The rACCD was purified by Ni-NTA purification system. The active form of rACCD having enzyme activity converted ACC to a-ketobutyrate. The optimal pH for ACC deaminase activity was pH 8.5, but no activity below pH 7.0 and a less severe tapering activity at base condition resulting in loss of activity at over pH 11. The optimal temperature of the enzyme was
Keywords
- 1-Aminocycloprophane-1-carboxlyate deaminase;
- Pseudomonas flourescens;
- Plant growth-promoting rhizobacteria;
- Enzymatic characterization;
- Recombinant Protein Expression