Discovery of D-Stereospecific Dipeptidase from Thermophilic Bacillus sp. BCS-l and Its Application for Synthesis of D-Amino Acid-Containing Peptide

  • Baek, Dae-Heoun (Microbial Conversion Research Unit, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Kwon, Seok-Joon (Microbial Conversion Research Unit, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Park, Jin-Seo (Microbial Conversion Research Unit, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Lee, Seung-Goo (Microbial Conversion Research Unit, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Mheen, Tae-Ick (Microbial Conversion Research Unit, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Sung, Moon-Hee (Microbial Conversion Research Unit, Korea Research Institute of Bioscience and Biotechnology (KRIBB))
  • Published : 1999.10.01

Abstract

A thermophilic bacterium producing D-stereospecific dipeptidase was isolated from Korean soil samples. The enzyme hydrolyzed the peptide bond between D-alanyl-D-alanine (D-Ala-D-Ala). The isolated bacterial strain was rod shaped, gram-positive, motile, and formed an endospore. Morphological and physiological characteristics suggested this microorganism a thermophilic Bacillus species, and was named as Bacillus sp. BCS-l. The production of D-stereospecific dipeptidase was growth-associated and optimal at $55^{\circ}C$. The enzyme was applied for the synthesis of D-amino acid-containing peptide, N-benzyloxycarbonyl-L-aspartyl-D-alanine benzyl ester (Z-L-Asp-D-AlaOBzl), as a model reaction. A thermodynamically controlled synthesis of Z-L-Asp-D-AlaOBzl was achieved in an organic solvent.

Keywords

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