Biotechnology and Bioprocess Engineering:BBE

  • 제9권4호
  • /
  • Pages.318-322
  • /
  • 2004
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  • 1226-8372(pISSN)
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  • 1976-3816(eISSN)
한국생물공학회 (The Korean Society for Biotechnology and Bioengineering)
권호 표지

Cloning and Characterization of the Lactate Dehydrogenase Genes from Lactobacillus sp. RKY2

  • Lee, Jin-Ha (Engineering Research Institute) ;
  • Choi, Mi-Hwa (Department of Material and Biochemical Engineering) ;
  • Park, Ji-Young (Department of Material and Biochemical Engineering) ;
  • Kang, Hee-Kyoung (Engineering Research Institute) ;
  • Ryu, Hwa-Won (School of Biological Sciences and Technology and Research Institute for Catalysis) ;
  • Sunwo, Chang-Sin (School of Biological Sciences and Technology and Research Institute for Catalysis) ;
  • Wee, Young-Jung (Department of Material and Biochemical Engineering) ;
  • Park, Ki-Deok (Korea Basic Science Institite Gwang-Ju Barnch, Chonnam National University) ;
  • Kim, Do-Won (Department of Physics, Kangnung National University) ;
  • Kim, Do-Man (Engineering Research Institute, School of Biological Sciences and Technology and Research Institute for Catalysis, Biology Research Center for Industrial Accelerator, Dongshin University)
  • 발행 : 2004.07.01
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초록

Lactic acid is an environmentally benign organic acid that could be used as a raw material for biodegradable plastics if it can be inexpensively produced by fermentation. Two genes (ldhL and ldhD) encoding the L-(+) and D-(-) lactate dehydrogenases (L-LDH and D-LDH) were cloned from Lactobacillus sp., RKY2, which is a lactic acid hyper-producing bacterium isolated from Kimchi. Open reading frames of ldhL for and ldhD for the L and D-LDH genes were 962 and 998 bp, respectively. Both the L(+)- and D(-)-LDH proteins showed the highest degree of homology with the L- and D-lactate dehydrogenase genes of Lactobacillus plantarum. The conserved residues in the catalytic activity and substrate binding of both LDHs were identified in both enzymes.

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참고문헌

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