서지주요정보
Erwinia rhapontici 돌연변이주와 재조합 E. coli를 이용한 Isomaltulose의 생산 = Production of isomaltulose by Erwinia rhapontici mutant and recombinant E. coli
서명 / 저자 Erwinia rhapontici 돌연변이주와 재조합 E. coli를 이용한 Isomaltulose의 생산 = Production of isomaltulose by Erwinia rhapontici mutant and recombinant E. coli / 최원.
저자명 최원 ; Choi, One
발행사항 [대전 : 한국과학기술원, 2000].
Online Access 원문보기 원문인쇄

소장정보

등록번호

8010710

소장위치/청구기호

학술문화관(문화관) 보존서고

MBS 00027

SMS전송

도서상태

이용가능

대출가능

반납예정일

초록정보

Isomaltulose synthase(EC. 5. 4. 99. 11) is an intracellular enzyme which converts sucrose to isomaltulose and trehalulose. In this study, mutants of Erwinia rhapontici and recombinant E. coli were developed for the production of isomaltulose with an enhanced activity of isomaltulose synthase. By NTG treatment, a mutant, E. rhapontici 27B4, was screened and the enzyme activity was increased from 75.5 U/mg to 80.4 U/mg compared to the wild type. The whole cells were immobilized with Ca-alginate as a bead form. The size of Ca-alginate beads did not affect the conversion of sucrose to isomaltulose. However, as the molecular weight of alginate decreased, the reaction rate and conversion yield were slightly increased. When a mutant 27B4 was used for the production of isomaltulose, the operational stability was slightly decreased compared with that of wild strain. The Isomaltulose synthase gene of E.rhapontici was fully cloned (1,800 bp) from the partial sequences (1,300 bp) that has been reported previously. And a recombinant E. coli was constructed with an expression vector pET16. Using a recombinant E. coli, culture conditions were optimized for the maximization of isomaltulose synthase ctivity. Sucrose was found to be the most suitable carbon source in an aspect of enzyme expression level and activity. Using 2 % sucrose as carbon source with 0.4 mM IPTG for 10 hours culture, the enzyme activity expressed was increased to 77. 4 U/mg, which was comparable to that of original strain, E. rhapontici. It was also found that most of protein expressed was remained as an inclusion body rather than a soluble form. Further study will be carried out in order to increase the soluble form of isomaltulose synthase.

서지기타정보

서지기타정보
청구기호 {MBS 00027
형태사항 v, 43 p. : 삽도 ; 26 cm
언어 한국어
일반주기 저자명의 영문표기 : One Choi
지도교수의 한글표기 : 김정회
지도교수의 영문표기 : Jung-Hoe Kim
학위논문 학위논문(석사) - 한국과학기술원 : 생물과학과,
서지주기 참고문헌 : p. 41-43
주제 이소말툴로오스
글루코실트랜스퍼라제
어위니아
팔라티노오스
고정화
Isomaltulose
Glucosyltransferase
Erwinia
Palatinose
Immobilization
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