남극톡토기 Cryptopygus antarcticus 의 베타-1,4-D-만난아제 효소의 특성

Title
남극톡토기 Cryptopygus antarcticus 의 베타-1,4-D-만난아제 효소의 특성
Alternative Title
Characterization of β-1,4-D-mannanase from the Antarctic springtail, Cryptopygus antarcticus
Author(s)
송정민; 남기웅; 강성균; 권석태; 김충곤; 이윤호
KIOST Author(s)
Kang, Sung Gyun(강성균)Kim, Choong Gon(김충곤)Lee, Youn Ho(이윤호)
Alternative Author(s)
송정민; 강성균; 김충곤; 이윤호
Publication Year
2007-10-19
Abstract
Abstract: The gene encoding a β-1,4-D-mannanase (CaMan) was identified from the ESTs of the Antarctic springtail, Cryptopygus antarcticus. The open reading frame consists of 1,149 bp encoding 382 amino acids with a putative signal peptide of 21 amino acids. It belongs to subfamily 10 of the glycoside hydrolase (GH) family 5. CaMan showed typical features of the cold active enzyme: it had high frequency of polar residues such as Asn, Gln and Ser, and a low ratio of Arg/(Arg+Lys) compared to the homologous mesophilic mollusc β-mannanases. The gene was fused with the thioredoxin gene in the pET-32a(+) and expressed in E. coli Rosetta-gami (DE3) as a catalytically active fusion protein (Trx-CaMan). The fusion protein was digested by thrombin and CaMan was purified. CaMan had high specific activity (416.3 U/mg) toward locust bean gum at an optimal temperature of 30℃ and optimal pH 3.5. Its optimal temperature is the lowest among those of the known mannanases. This work was support by the Marine and Extreme Genome Research Center program of Maritime Affairs and Fisher, Republic of Korea.
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/30290
Bibliographic Citation
2007 추계 한국분자세포생물학회, pp.409, 2007
Publisher
한국분자세포생물학회
Type
Conference
Language
English
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