Earticle

초록

영어

The Full gene of Paenibacillus sp. dextranase was open reading frame comprises of 5,091 bp encoding 1,696 amino acids. The primary structure of PDEX has 30% identity with CITase from Bacillus circulans and shows 10-15% identities with Streptococcus dextranases. PDEX has a catalytic domain and three-repeated cell surface layer homology (SLH) domains at the C-terminus. GH family 66 enzymes have the nine conserved regions, which may be important for their enzyme activities. CITase or PDEX has a long insertion part, especially the insertion of PDEX is very long. These amino acids may contribute to the synthesis of CI. SLH domains might be responsible for binding of cell wall. PDEX has proline rich region between catalytic domain and SLH domains, which seems to be a linker. PDEX produces CIs as well as isomaltooligosaccharides from dextran in the initial stage of enzyme reaction. The cyclic structure of CIs is determined by 1H-NMR and 13C-NMR. ESI-MS analysis confirms that CIs are composed of 7-14 glucosyl units.

저자

• Young-Min Kim [ Laboratory of Functional Carbohydrate Enzymes and Microbial Genomics, School of Biological Sciences and Technology, Chonnam National University ]
• Yun Lee [ Laboratory of Functional Carbohydrate Enzymes and Microbial Genomics, School of Biological Sciences and Technology, Chonnam National University ]
• Jin Kang [ Laboratory of Functional Carbohydrate Enzymes and Microbial Genomics, School of Biological Sciences and Technology, Chonnam National University ]
• Doman Kim [ Laboratory of Functional Carbohydrate Enzymes and Microbial Genomics, School of Biological Sciences and Technology, Chonnam National University ]
• Kimura Atsuo [ Molecular Enzymology Laboratory, Research Faculty of Agriculture, Hokkaido University ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576