Yu-Ri LIM, Ran-Young YOON, Eun-Seon SEO, Yeong-Su KIM, Chang-Su PARK, Deok-Kun OH
언어
영어(ENG)
URL
https://www.earticle.net/Article/A115067
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원문정보
초록
영어
A recombinant α-l-arabinofuranosidase from Caldicellulosiruptor saccharolyticus was purified by heat treatment and Hi-Trap anion exchange chromatography with a specific activity of 28.2 U mg−1. The native enzyme was a 58-kDa octamer with a molecular mass of 460 kDa, as measured by gel filtration. The catalytic residues and consensus sequences of the glycoside hydrolase 51 family of α-l-arabinofuranosidases were completely conserved in α-l-arabinofuranosidase from C. saccharolyticus. The maximum enzyme activity was observed at pH 5.5 and 80ºC with a half-life of 49 h at 75ºC. Among aryl-glycoside substrates, the enzyme displayed activity only for p-nitrophenyl-α-l-arabinofuranoside, with a maximum kcat/Km of 220 mM–1 s–1, and p-nitrophenyl-α-l-arabinopyranoside. No activity was observed for arabinan or debranched arabinan. This substrate specificity differs from those of other α-l-arabinofuranosidases. In a 1 mM solution of each sugar, arabino-oligosaccharides with two to five monomer units were completely hydrolyzed to l-arabinose within 13 h in the presence of 30 U ml−1 of enzyme at 75ºC. The novel substrate specificity and hydrolytic properties for arabino-oligosaccharides demonstrate the potential of α-l-arabinofuranosidase from C. saccharolyticus for use in the commercial production of l-arabinose.
한국생물공학회 [The Korean Society for Biotechnology and Bioengineering]
설립연도
1984
분야
공학>생물공학
소개
이 법인은 생물 공학의 발전과 보급에 이바지하고, 회원 상호 간의 연구 협력과 친목을 도모함을 목적으로 한다
1. 생물공학 분야의 발전을 위한 연구 협력
2. 생물공학의 실용화를 촉진시키기 위한 산학 협동
3. 학술연구 발표회, 강연회, 연수회 등 학술활동의 개최
4. 국,영문 학술지,소식지,학술회의 Proceedings 및 학술도서의 발간
5. 생물공학 발전을 위한 정책 건의
6. 기타 국제 교류 등 본 학회의 목적 달성을 위한 제반 활동