Production of Non-Proteinaceous Amino Acids using Recombinant <I>E. coli</I> Cells

• Nakanishi Kazuhiro

  Department of Bioscience and Biotechnology, Okayama University, Japan

• Zhao Chunhui

  Department of Bioscience and Biotechnology, Okayama University, Japan

• Imamura Koreyoshi

  Department of Bioscience and Biotechnology, Okayama University, Japan

• Ohno Katsuhiro

  Department of Bioscience and Biotechnology, Okayama University, Japan

抄録

β-(Pyrazol-1-yl)-L-alanine (β-pyrazole-L-Ala; β-PA), a model non-proteinaceous amino acid was synthesized using recombinant Escherichia coli cells that express cysteine synthase and enzymes that regenerate acetyl-CoA. In Method A, β-PA was synthesized from L-Ser and pyrazole using recombinant cells that express wild-type serine acetyltransferase (SAT), O-acetylserine sulfhydrylase-A (OASS-A), acetate kinase (AK), and phosphotransacetylase (PTA). Under the optimized condition, β-PA was produced at 140 mM from 200 mM L-Ser and 200 mM pyrazole. On the other hand, in Method B, O-acetyl-L-serine (OAS) was secreted into the broth, using the cells that express SATΔC20 (truncated SAT), OASS-A, AK, and PTA. Under optimized conditions OAS accumulated in the broth at levels of around 100 mM. The secreted OAS was efficiently converted to β-PA at levels of around 90 mM from 105 mM OAS using free OASS-A. In both Methods A and B, the addition of glucose was essential for the efficient production of β-PA and OAS, respectively.

収録刊行物

• アジア・太平洋化学工学会議発表論文要旨集

  アジア・太平洋化学工学会議発表論文要旨集 2004 (0), 815-815, 2004

  公益社団法人 化学工学会

キーワード

• cysteine synthase
• <I>E. coli</I>
• <I>O</I>-acetyl-L-serine
• β-pyrazole-L-alanine
• non-proteinaceous amino acid

詳細情報

• CRID: 1390282680709554176
• NII論文ID: 130005052902
• DOI: 10.11491/apcche.2004.0.815.0
• 本文言語コード: en
• データソース種別:
  • JaLC
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可