기관회원 [로그인]
소속기관에서 받은 아이디, 비밀번호를 입력해 주세요.
개인회원 [로그인]

비회원 구매시 입력하신 핸드폰번호를 입력해 주세요.
본인 인증 후 구매내역을 확인하실 수 있습니다.

회원가입
서지반출
Development of a Food-Grade Integration Vector for Heterologous Gene Expression and Protein Secretion in Lactococcus lactis
[STEP1]서지반출 형식 선택
파일형식
@
서지도구
SNS
기타
[STEP2]서지반출 정보 선택
  • 제목
  • URL
돌아가기
확인
취소
  • Development of a Food-Grade Integration Vector for Heterologous Gene Expression and Protein Secretion in Lactococcus lactis
  • Development of a Food-Grade Integration Vector for Heterologous Gene Expression and Protein Secretion in Lactococcus lactis
저자명
Jeong. Do-Won,Lee. Jong-Hoon,Kim. Kyoung-Heon,Lee. Hyong-Joo
간행물명
Journal of microbiology and biotechnology
권/호정보
2006년|16권 11호|pp.1799-1808 (10 pages)
발행정보
한국미생물생명공학회
파일정보
정기간행물|ENG|
PDF텍스트
주제분야
기타
이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
서지반출

기타언어초록

A food-grade integration vector based on site-specific recombination was constructed. The 5.7-kb vector, pIMA20, contained an integrase gene and a phage attachment site originating from bacteriophage A2, with the ${alpha}$-galactosidase gene from Lactobacillus plantarum KCTC 3104 as a selection marker. pIMA20 was also equipped with a controllable promoter of nisA ($P_{nisA}$) and a signal peptide-encoding sequence of usp45 ($SP_{usp45}$) for the production and secretion of foreign proteins. pIMA20 and its derivatives mediated site-specific integration into the attB-like site on the Lactococcus lactis NZ9800 chromosome. The vector-integrated recombinant lactococci were easily detected by the appearance of blue colonies on a medium containing $X-{alpha}-gal$ and also by their ability to grow on a medium containing melibiose as the sole carbon source. Recombinant lactococci maintained these traits in the absence of selection pressure during 100 generations. The ${alpha}-amylase$ gene from Bacillus licheniformis, lacking a signal peptide-encoding. sequence, was inserted downstream of $P_{nisA};and;SP_{usp45}$ in pIMA20, and the plasmid was integrated into the L. lactis chromosome. ${alpha}-Amylase$ was successfully produced and secreted by the recombinant L. lactis, controlled by the addition and concentration of nisin.