Earticle

초록

영어

Clostridium beijerinckii NCIMB 8052 as a butanol producer contains plenty of hydrolase and is able to utilize wide spectrum of carbohydrates. A 1,3-β-D-glucanase gene, which is annotated as Cbei_2828, was cloned from Clostridium beijerinckii NCIMB 8052 and expressed and purified in Escherichia coli BL21 (DE3). This glucanase gene has 1,362 base pairs and encodes a protein of 410 amino acids with a calculated molecular mass of 45 kDa. Signal peptideof this hydrolase was not cloned, so the total expressed protein has a molecular mass of 42 kDa. The encoded protein comprises a catalytic domain of glycosyl hydrolase family 16, fibronectin type 3 domain and Chitin/cellulose binding domain. The expressed enzyme was characterized. The activity of the expressed protein was tested by zymography and TLC by incubating the crude enzyme in Tris-Cl buffer containing 1% laminarin (w/v). The optimum working temperature and pH, substrate specificity and thermal stability of the purified enzyme will be tested. Kinetic parameters such as Km value and Vmaxwill also be evaluated.

키워드

저자

• Pan LI [ Dept.of Chemical Engineering, Sungkyunkwan University. ]
• Byong-Woo KIM [ Dept.of Chemical Engineering, Sungkyunkwan University. ]
• Jae Hyuk CHUNG [ Department of Biotechnology,Korea University. ]
• Heetaek KIM [ Department of Biotechnology,Korea University. ]
• Kyoung Heon KIM [ Department of Biotechnology,Korea University. ]
• Jieun LEE [ Department of Biotechnology,Korea University. ]

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발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576