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Cloning and expression of S-Adenosyl Methionine Synthetase gene in recombinant E. coli strain for large scale production of SAMe
Detchanamurthy, Swaminathan; Shanmugam, Kirubanandan; Parkunan, Salai Madhumathi Arasi; Puttananjaiah, Shilpa; Somasundaram, Balaji; Subramanian, Kannan.
Affiliation
  • Detchanamurthy, Swaminathan; Sri Venkateswara College of Engineering. Department of Biotechnology. Bioprocess and Downstream Processing Laboratory. Sriperumbudur. IN
  • Shanmugam, Kirubanandan; Sri Venkateswara College of Engineering. Department of Biotechnology. Bioprocess and Downstream Processing Laboratory. Sriperumbudur. IN
  • Parkunan, Salai Madhumathi Arasi; Sri Venkateswara College of Engineering. Department of Biotechnology. Bioprocess and Downstream Processing Laboratory. Sriperumbudur. IN
  • Puttananjaiah, Shilpa; University of Mysore. Department of Biotechnology. Mysore. IN
  • Somasundaram, Balaji; University of Canterbury. Department of Chemical and Process Engineering. Christchurch. NZ
  • Subramanian, Kannan; University of Canterbury. Department of Chemical and Process Engineering. Christchurch. NZ
Electron. j. biotechnol ; 13(4): 1-2, July 2010. ilus, tab
Article in En | LILACS | ID: lil-577106
Responsible library: CL1.1
ABSTRACT
S-Adenosyl Methionine (SAMe) Synthetase is an enzyme which catalyses the synthesis of S-Adenosyl Methionine using methionine and ATP. It is also known as AdoMet which is well known methyl donor, which modifies DNA, RNA, histones and other proteins, dictating replicational, transcriptional and translational fidelity, mismatch repair, chromatin modeling, epigenetic modifications and imprinting. The objective of the present work is to clone the SAMe Synthetase gene in recombinant E. coli strain in order to express, characterize and purify it for further synthesis of SAMe in a large scale fermentation. Expression was induced by 1 mM IPTG and expressed protein was characterized by SDS-PAGE. The recombinant E. coli cells were used for the production of SAMe through batch and fed batch fermentation operations. The produced SAMe was purified through paper chromatography in order to use it in our future studies.
Subject(s)

Full text: 1 Collection: 01-internacional Database: LILACS Main subject: Cloning, Molecular / Escherichia coli / Fermentation / Methionine Adenosyltransferase Language: En Journal: Electron. j. biotechnol Journal subject: BIOTECNOLOGIA Year: 2010 Document type: Article Affiliation country: /

Full text: 1 Collection: 01-internacional Database: LILACS Main subject: Cloning, Molecular / Escherichia coli / Fermentation / Methionine Adenosyltransferase Language: En Journal: Electron. j. biotechnol Journal subject: BIOTECNOLOGIA Year: 2010 Document type: Article Affiliation country: /