High Yield Synthesis of 12-Aminolauric Acid by "Enzymatic Transcrystallization" of .OMEGA.-Laurolactam Using .OMEGA.-Laurolactam Hydrolase from Acidovorax sp. T31

• FUKUTA Yasuhisa

  Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University

• KOMEDA Hidenobu

  Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University

• YOSHIDA Yoichi

  Research and Development Headquarters of Ubekousan, Ubekousan

• ASANO Yasuhisa

  Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University

Bibliographic Information

Other Title

• High yield synthesis of 12-aminolauric acid by "enzymatic transcrystallization" of ω-laurolactam using ω-laurolactam hydrolase from Acidovorax sp. T31
• High yield synthesis of 12 aminolauric acid by enzymatic transcrystallization of o laurolactam using o laurolactam hydrolase from Acidovorax sp T31
• High Yield Synthesis of 12-Aminolauric Acid by “Enzymatic Transcrystallization” of ω-Laurolactam Using ω-Laurolactam Hydrolase from<i>Acidovorax</i>sp. T31

Abstract

The genes encoding ω-laurolactam hydrolases from Cupriavidus sp. T7, Acidovorax sp. T31, Cupriavidus sp. U124, and Sphingomonas sp. U238 were cloned and sequenced. Nucleotide and amino acid sequence analysis of the four genes indicated that the primary structures of these ω-laurolactam hydrolases are significantly similar to the 6-aminohexanoate-cyclic-dimer hydrolase (EC 3.5.2.12). These genes were expressed in Escherichia coli, and the ω-laurolactam hydrolysing activity of the recombinant enzymes was compared with that of 6-aminohexanoate-cyclic-dimer hydrolase from Arthrobacter sp. KI72. The enzyme from Acidovorax sp. T31 was most successfully expressed in E. coli. Cell-free extract of the recombinant strain was used for the synthesis of 12-aminolauric acid from ω-laurolactam by “enzymatic transcrystallization,” because crystalline ω-laurolactam added into the enzyme solution was converted to crystalline 12-aminolauric acid (≧97.3% yield). Under the optimum conditions, 208 g/l of 12-aminolauric acid was produced in 17 h. The resulting pure product was identical to authentic 12-aminolauric acid.

Journal

• Bioscience, Biotechnology, and Biochemistry

  Bioscience, Biotechnology, and Biochemistry 73 (5), 980-986, 2009

  Japan Society for Bioscience, Biotechnology, and Agrochemistry

Keywords

• enzymatic transcrystallization
• ω-laurolactam
• 12-aminolauric acid
• <I>Acidovorax</I> sp.
• 6-aminohexanoate-cyclic-dimer hydrolase

Details

• CRID: 1390282681453687040
• NII Article ID: 10027540396
• NII Book ID: AA10824164
• DOI: 10.1271/bbb.80551
• ISSN: 13476947
• ISSN: 09168451
• NDL BIB ID: 10234407
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I10234407
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.80551
• Text Lang: en
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed