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

Soojin Lee; Borim Kim; Minkyu Oh; Youngrok Kim; Jinwon Lee

doi:10.1007/s00449-012-0824-z

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

Soojin Lee, Borim Kim, Minkyu Oh, Youngrok Kim, Jinwon Lee

Department of Chemical and Biological Engineering

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	1005-1010
Number of pages	6
Journal	Bioprocess and Biosystems Engineering
Volume	36
Issue number	7
DOIs	https://doi.org/10.1007/s00449-012-0824-z
Publication status	Published - 2013 Jul

Keywords

2,3-Butanediol
Codon optimization
Escherichia coli
Gene expression
Meso-secondary alcohol dehydrogenase

ASJC Scopus subject areas

Biotechnology
Bioengineering

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title = "Enhanced activity of meso-secondary alcohol dehydrogenase from Klebsiella species by codon optimization",

abstract = "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.",

keywords = "2,3-Butanediol, Codon optimization, Escherichia coli, Gene expression, Meso-secondary alcohol dehydrogenase",

author = "Soojin Lee and Borim Kim and Minkyu Oh and Youngrok Kim and Jinwon Lee",

note = "Funding Information: Acknowledgments This research was supported by the R&D Program of MKE/KEIT (No. 10035578, Development of 2,3-butanediol and derivative production technology for C-Zero bio-platform industry). Funding Information: This work was supported by the Graduate School of Specialization for Biotechnology Program of the Ministry of Knowledge Economy (MKE).",

year = "2013",

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doi = "10.1007/s00449-012-0824-z",

language = "English",

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AU - Lee, Soojin

AU - Kim, Borim

AU - Oh, Minkyu

AU - Kim, Youngrok

AU - Lee, Jinwon

N1 - Funding Information: Acknowledgments This research was supported by the R&D Program of MKE/KEIT (No. 10035578, Development of 2,3-butanediol and derivative production technology for C-Zero bio-platform industry). Funding Information: This work was supported by the Graduate School of Specialization for Biotechnology Program of the Ministry of Knowledge Economy (MKE).

PY - 2013/7

Y1 - 2013/7

N2 - 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.

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

Abstract

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