Journal of Life Science (생명과학회지)

Korean Society of Life Science (한국생명과학회)
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Cloning, Purification and Characterization of Novel L-Aspartate β-decarboxylase from Enterococcus

Enterococcus faecalsis 유래의 신규 L-aspartate β-decarboxylase의 cloning, 정제 및 활성 규명

  • Lee Dong-Geun (Department of Bioscience and Biotechnology, College of Engineering, Silla University) ;
  • Song Tae-Yoon (Department of Bioscience and Biotechnology, College of Engineering, Silla University) ;
  • Kim Nam Young (Department of Bioscience and Biotechnology, College of Engineering, Silla University) ;
  • Lee Eo-Jin (Department of Bioscience and Biotechnology, College of Engineering, Silla University) ;
  • Ha Sang-An (Department of Environmental Engineering, College of Engineering, Silla University) ;
  • Lee Jae-Hwa (Department of Bioscience and Biotechnology, College of Engineering, Silla University) ;
  • Ha Jong-Myuong (Department of Bioscience and Biotechnology, College of Engineering, Silla University) ;
  • Ha Bae Jin (Department of Bioscience and Biotechnology, College of Engineering, Silla University) ;
  • Lee Sang-Hyeon (Department of Bioscience and Biotechnology, College of Engineering, Silla University)
  • 이동근 (신라대학교 공과대학 생명공학과) ;
  • 송태윤 (신라대학교 공과대학 생명공학과) ;
  • 김남영 (신라대학교 공과대학 생명공학과) ;
  • 이어진 (신라대학교 공과대학 생명공학과) ;
  • 하상안 (신라대학교 공과대학 환경공학과) ;
  • 이재화 (신라대학교 공과대학 생명공학과) ;
  • 하종명 (신라대학교 공과대학 생명공학과) ;
  • 하배진 (신라대학교 공과대학 생명공학과) ;
  • 이상현 (신라대학교 공과대학 생명공학과)
  • Published : 2006.02.01
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Abstract

The gene for a L-aspartate $\beta-decarboxylase$ (ADC) from Enterococcus faecalis was cloned and sequenced. The gene comprised an open reading frame of 1,611 base pairs, which encodes a protein of 58,960 Da consisting of 536 amino acid residues. The gene was subcloned into an expression plasmid for overexpression of the ADC. The recombinant ADC was produced using E. coli as the host and purified to homogeneity. Our result showed that the ADC may be obtained from bacteria known nucleotide sequence. Thus, we suggest that high value L-alanine might be produced by low value aspartate.

L-alanine의 산업적 생산을 위한 신규의 L-aspartate $\beta-carboxylase$ 유전자를 Enterococcus faecalis에서 검색하고 이를 대장균에 형질전환시켰다. E. faecalis 유래의 ADC유전자 는 1611 bp의 염기서열로 구성되어 있으며 형질전환된 대장균에서 59 KDa의 효소를 생산하며 L-aspartate $\beta-carboxylase$의 촉매활성을 나타내는 것을 확인하였다. 본 연구결과로 기능은 모르고 유전체 서열만 아는 균체에서 신규 효소를 개발하는 방법을 확립하였으며 저가의 aspartate를 이용한 고부가가치 L-alanine을 생산할 수 있는 신규효소를 개발할 수 있었다.

Keywords

References

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