Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Purification and Characterization of a New Peptidase, Bacillopeptidase DJ-2, Having Fibrinolytic Activity: Produced by Bacillus sp. DJ-2 from Doen-Jang

  • CHOI, NACK-SHICK (Proteome and Research Laboratory, Korea Research Institute of Bioscience and Biotechnology, Department of Microbiology, Chungnam National University) ;
  • YOO, KI-HYUN (Proteome and Research Laboratory, Korea Research Institute of Bioscience and Biotechnology) ;
  • HAHM, JEUNG-HO (Proteome and Research Laboratory, Korea Research Institute of Bioscience and Biotechnology) ;
  • YOON, KAB-SEOG (Proteome and Research Laboratory, Korea Research Institute of Bioscience and Biotechnology) ;
  • CHANG, KYU-TAE (Primate Research Laboratory, Korea Research Institute of Bioscience and Biotechnology) ;
  • HYUN, BYUNG-HWA (Primate Research Laboratory, Korea Research Institute of Bioscience and Biotechnology) ;
  • PIL, JAE-MAENG (Department of Microbiology, Chungnam National University) ;
  • KIM, SEUNG-HO (Proteome and Research Laboratory, Korea Research Institute of Bioscience and Biotechnology)
  • Published : 2005.02.01
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Abstract

A new Bacillus peptidase, bacillopeptidase DJ-2 (bpDJ-2), with molecular mass of 42 kDa and isoelectric point (pI) of 3.5- 3.7, was purified to homogeneity from Bacillus sp. DJ-2 isolated from Doen-Jang, a traditional Korean soybean fermented food. The enzyme was identified as an extracellular serine fibrinolytic protease. The optimal conditions for the reaction were pH 9.0 and $60^{\circ}C$. The first 18 amino acid residues of the N-terminal amino acid sequence of bpDJ-2 were TDGVEWNVDQIDAPKAW, which is identical to that of bacillopeptidase F (bpf). However, based on their Nterminal amino acid sequence, molecular size, and pI, it is different from that of bpf and extracellular 90 kDa. The whole (2,541 bp, full-bpDJ-2) and mature (1,956 bp, mature-bpDJ-2) genes were cloned, and its nucleotide sequence and deduced amino acid sequence were determined. The expressed proteins, full-bpDJ-2 and mature-bpDJ-2, were detected on SDSPAGE at expected sizes of 92 and 68 kDa, respectively.

Keywords

References

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