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Discovery of D-Stereospecific Dipeptidase from Thermophilic Bacillus sp. BCS-l and Its Application for Synthesis of D-Amino Acid-Containing Peptide
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  • Discovery of D-Stereospecific Dipeptidase from Thermophilic Bacillus sp. BCS-l and Its Application for Synthesis of D-Amino Acid-Containing Peptide
  • Discovery of D-Stereospecific Dipeptidase from Thermophilic Bacillus sp. BCS-l and Its Application for Synthesis of D-Amino Acid-Containing Peptide
저자명
Baek. Dae-Heoun,Kwon. Seok-Joon,Park. Jin-Seo,Lee. Seung-Goo,Mheen. Tae-Ick,Sung. Moon-Hee
간행물명
Journal of microbiology and biotechnology
권/호정보
1999년|9권 5호|pp.646-649 (4 pages)
발행정보
한국미생물생명공학회
파일정보
정기간행물|ENG|
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이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
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기타언어초록

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.