Enzymatic Synthesis of L-Tryptophan by Enterobacter aerogenes Tryptophanase Highly Expressed in Escherichia coli, and Some Properties of the Purified Enzyme

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概要

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• We constructed two plasmids that have a strong tac promoter and a structural gene for tryptophanase of Enterobacter aerogenes SM-18 (pKT901EA) or Escherichia coli K-12 (pKT951EC). The tryptophanase activity of E. coli JM109 transformed with pKT901EA (JM109/pKT901EA) was inducible with isopropyl-β-D-thiogalactopyranoside, and 3. 6 times higher than that of E. aerogenes SM-18. Cells of JM109/pKT901EA induced for tryptophanase synthesized L-tryptophan from indole, ammonia, and Pyruvate more efficiently than E. aerogenes SM-18. Although JM109/pKT951EC expressed a similar level of tryptophanase activity to that of JM109/pKT901EA, the synthesis of L-tryptophan by the cells of JM109/pKT951EC did not proceed well compared with JM109/pKT901EA. Tryptophanases from E. aerogenes and E. coli K-12 were purified, and their properties were investigated. The purified E. aerogenes tryptophanase showed higher stability against heat inactivation than E. coli tryptophanase.

• 社団法人日本農芸化学会の論文
• 1995-10-23

著者

• Yokota Atsushi

  Laboratory of Microbial Physiology, Research Faculty of Agriculture, Hokkaido University

• TOMITA FUSAO

  Laboratory of Applied Microbiology, Graduate School of Agriculture, Hokkaido University

• Yokota A

  Laboratory Of Applied Microbiology Department Of Bioscience And Chemistry Faculty Of Agriculture Hok

• Yokota Atsushi

  Laboratory Of Applied Microbiology Department Of Bioscience And Chemistry Faculty Of Agriculture Hok

• Tomita Fusao

  Laboratory Of Applied Microbiology

• Kawasaki Kosei

  Laboratory of Applied Microbiology, Department of Bioscience and Chemistry, Faculty of Agriculture,

• Yokota A

  Hokkaido Univ. Hokkaido Jpn

• Kawasaki K

  Bioscience And Chemistry Division Hokkaido National Industrial Research Institute Aist

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