Earticle

현재 위치 Home

Lignocellulose-based Saccharification and Biorefinery, Chair : Jong-In Han (KAIST, Korea)

Binding Characteristics of a Bacterial Expansin (BsEX LX 1 )to M icro cry stalline Cellulo se and Pretreated Lignocellulose

첫 페이지 보기
  • 발행기관
    한국생물공학회 바로가기
  • 간행물
    한국생물공학회 학술대회 바로가기
  • 통권
    2012 춘계학술대회 및 국제심포지움 (2012.04)바로가기
  • 페이지
    pp.88-88
  • 저자
    Kyoung Heon KIM, Jinhua XUAN, In Jung KIM, Hee Jin LEE, Young Hoon JUNG, In-Geol CHOI
  • 언어
    영어(ENG)
  • URL
    https://www.earticle.net/Article/A174050

※ 원문제공기관과의 협약기간이 종료되어 열람이 제한될 수 있습니다.

원문정보

초록

영어
Plant expansins are capable of inducing plant cell wall extension and disrupting cellulose. BsEXLX1 found in Bacillus subtilis is a bacterial expansin, a structural homolog to a plant expansin ZmEXPB1. In our previous study, BsEXLX1was found to possess synergism with cellulase in the enzymatic hydrolysis of cellulose (Kim, E. S. et al., 2009, Biotechnol. Bioeng. 102(5):1342-1353). The thermodynamic analysis of binding of BsEXLX1 to micrcrystalline cellulose (e.g., Avicel) revealed that the binding mode of BsEXLX1 to Avicel was similar to those of other Type A surface-binding carbohydrate binding modules (CBMs). BsEXLX1 bound to Avicel in an entropy-driven mode possibly due to the increased mobility of water molecules released from the interface between the protein and the substrate. BsEXLX1 did not bind to soluble cellooligosaccharides, which was also similar to the behavior of other Type A CBMs. In addition, cellulose and xylan had much lower binding for BsEXLX1 than for CtCBD3, a Type A CBM. When the binding studies of BsEXLX1 were performed against pretreated or unpretreated Miscanthus x giganteus using CtCBD3, the amounts of BsEXLX1 bound to lignin-rich substrates were much higher compared to those of CtCBD3. Also, a binding competition assay demonstrated BsEXLX1 binding decreased in the presence of CtCBD3 against Avicel but not against alkali lignin. The mutagenesis of each of the three hydrophobic amino acid residues on the binding domain on the C-terminus of BsEXLX1 that are presumed to be responsible for cellulose binding did not affect the lignin binding activity but substantially decreased the cellulose binding activity. The findings in this work suggest that BsEXLX1 could be industrially applicable as a lignin blocker during the enzymatic hydrolysis of lignocellulose.

키워드

Expansin Cellulose Binding Lignocellulose

저자

  • Kyoung Heon KIM [ School of Life Sciences and Biotechnology, Korea University, Seoul 136-713. ]
  • Jinhua XUAN [ School of Life Sciences and Biotechnology, Korea University, Seoul 136-713. ]
  • In Jung KIM [ School of Life Sciences and Biotechnology, Korea University, Seoul 136-713. ]
  • Hee Jin LEE [ School of Life Sciences and Biotechnology, Korea University, Seoul 136-713. ]
  • Young Hoon JUNG [ School of Life Sciences and Biotechnology, Korea University, Seoul 136-713. ]
  • In-Geol CHOI [ School of Life Sciences and Biotechnology, Korea University, Seoul 136-713. ]

참고문헌

자료제공 : 네이버학술정보

간행물 정보

발행기관

  • 발행기관명
    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

간행물

  • 간행물명
    한국생물공학회 학술대회
  • 간기
    반년간
  • 수록기간
    1985~2013
  • 십진분류
    KDC 476 DDC 576

이 권호 내 다른 논문 / 한국생물공학회 학술대회 2012 춘계학술대회 및 국제심포지움

    피인용수 : 0(자료제공 : 네이버학술정보)

    함께 이용한 논문 이 논문을 다운로드한 분들이 이용한 다른 논문입니다.

      페이지 저장