Enhanced activity of meso-secondary alcohol dehydrogenase from Klebsiella species by codon optimization

Meso -secondary alcohol dehydrogenases ( meso -SADH) from Klebsiella oxytoca KCTC1686 and Klebsiella pneumoniae KCTC2242 were codon optimized and expressed in Escherichia coli W3110. The published gene data of K. pneumoniae NTUH-K2044 (NCBI accession number AP006725), K. pneumoniae 342 (NCBI accessi...

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Published in:Bioprocess and biosystems engineering 2013-07, Vol.36 (7), p.1005-1010
Main Authors: Lee, Soojin, Kim, Borim, Oh, Minkyu, Kim, Youngrok, Lee, Jinwon
Format: Article
Language:English
Subjects:
Alcohol Dehydrogenase - chemistry
Alcohol Dehydrogenase - genetics
Alcohol Dehydrogenase - metabolism
Bacteria
Base Sequence
Bioengineering
Biotechnology
Chemistry
Chemistry and Materials Science
Codon
DNA Primers
E coli
Electrophoresis, Polyacrylamide Gel
Environmental Engineering/Biotechnology
Enzymatic activity
Enzymes
Food Science
Gene expression
Industrial and Production Engineering
Industrial Chemistry/Chemical Engineering
Klebsiella - enzymology
Molecular Sequence Data
Plasmids
Sequence Homology, Nucleic Acid
Short Communication
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creator Lee, Soojin
Kim, Borim
Oh, Minkyu
Kim, Youngrok
Lee, Jinwon
description Meso -secondary alcohol dehydrogenases ( meso -SADH) from Klebsiella oxytoca KCTC1686 and Klebsiella pneumoniae KCTC2242 were codon optimized and expressed in Escherichia coli W3110. The published gene data of K. pneumoniae NTUH-K2044 (NCBI accession number AP006725), K. pneumoniae 342 (NCBI accession number CP000964), and K. pneumoniae MGH 78578 (NCBI accession number CP000647), were compared with the meso -SADH sequences of each strain, respectively. Codon-optimized meso -SADH enzymes of K. oxytoca and K. pneumoniae showed approximately twofold to fivefold increased enzyme activities for acetoin reduction over native enzymes. The highest activities for each strain were obtained at 30–37 °C and pH 6–7 (yielding 203.1 U/mg of protein and 156.5 U/mg of protein, respectively). The increased enzyme activity of the codon-optimized enzymes indicated that these modified enzymes could convert acetoin into 2,3-butanediol with a high yield.
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subjects Alcohol Dehydrogenase - chemistry
Alcohol Dehydrogenase - genetics
Alcohol Dehydrogenase - metabolism
Bacteria
Base Sequence
Bioengineering
Biotechnology
Chemistry
Chemistry and Materials Science
Codon
DNA Primers
E coli
Electrophoresis, Polyacrylamide Gel
Environmental Engineering/Biotechnology
Enzymatic activity
Enzymes
Food Science
Gene expression
Industrial and Production Engineering
Industrial Chemistry/Chemical Engineering
Klebsiella - enzymology
Molecular Sequence Data
Plasmids
Sequence Homology, Nucleic Acid
Short Communication
title Enhanced activity of meso-secondary alcohol dehydrogenase from Klebsiella species by codon optimization
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