서지주요정보
방향적 진화를 통한 알칼리 조건에서의 Xylanase의 활성과 안정성의 증가 = Enhancement of activity and stability of xylanase by directed evolution under alkaline condition
서명 / 저자 방향적 진화를 통한 알칼리 조건에서의 Xylanase의 활성과 안정성의 증가 = Enhancement of activity and stability of xylanase by directed evolution under alkaline condition / 고성필.
저자명 고성필 ; Ko, Seong-Pil
발행사항 [대전 : 한국과학기술원, 2004].
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소장정보

등록번호

8014826

소장위치/청구기호

학술문화관(문화관) 보존서고

MBS 04002

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초록정보

Endoxylanase catalyzes the hydrolysis of xylan, a plant cell wall heteropolysaccharide that contains a backbone of 1,4-linked xylose residues. Xylanases have been found to be effective in reducing chlorine dosage requirements in the pulp-bleaching process. It is desirable that xylanases used for industries are stable and active under alkaline conditions at high temperatures. In this study, the activity and stability of xylanases from Bacillus sp. were improved by directed evolution. Three evolved mutants were isolated after sequential rounds of error-prone PCR to introduce random mutations, and membrane-based screening of the resultant mutant library. They were identified as having one(mutant 3-5), two(mutant 6-8), and three(mutant 10-61) amino acid substitutions, respectively. All the substituted amino acids of mutant 10-61 were located on the protein surface, and had polar residues with hydroxyl group. Compared to the wild type enzyme, the stability of three mutants in alkaline condition were enhanced without the loss of specific activity. Mutant 10-61 was 2.5-fold more active than wild type enzyme after 30h incubation in Tris-CI buffer(pH 9.0). In addition to alkaline stability, thermostability was also improved in the three mutants.

서지기타정보

서지기타정보
청구기호 {MBS 04002
형태사항 vi, 44 p. : 삽도 ; 26 cm
언어 한국어
일반주기 저자명의 영문표기 : Seong-Pil Ko
지도교수의 한글표기 : 김정회
지도교수의 영문표기 : Jeong-Hoe Kim
학과명칭변경 : 생물과학과가 생명과학과로 변경됨
학위논문 학위논문(석사) - 한국과학기술원 : 생명과학과,
서지주기 참고문헌 : p. 37-41
주제 방향적 진화
알칼리
안정성
활성
스크리닝
DIRECTED EVOLUTION
XYLANASE
ALKALINE CONDITION
STABILITY
MEMBRANE-BASED SCREENING
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