메뉴 건너뛰기
.. 내서재 .. 알림
소속 기관/학교 인증
인증하면 논문, 학술자료 등을  무료로 열람할 수 있어요.
한국대학교, 누리자동차, 시립도서관 등 나의 기관을 확인해보세요
(국내 대학 90% 이상 구독 중)
로그인 회원가입 고객센터 ENG
주제분류

추천
검색

이용수

표지
📌
연구주제
📖
연구배경
🔬
연구방법
🏆
연구결과
AI에게 요청하기
추천
검색

초록· 키워드

오류제보하기
A direct approach was used to retrieve activelipases from Paenibacillus polymyxa genome databases.Twelve putative lipase genes were tested using a typical lipasesequence rule built on the basis of a consensus sequence of acatalytic triad and oxyanion hole. Among them, six genessatisfied the sequence rule and had similarity (about 25%)with known bacterial lipases. To obtain the six lipase proteins,lipase genes were expressed in E. coli cells and lipolyticactivities were measured by using tributyrin plate and pnitrophenylcaproate. One of them, contig 160-26, was expressedas a soluble and active form in E. coli cell. After purifying onNi-NTA column, its detailed biochemical properties werecharacterized. It had a maximum hydrolytic activity at 30oCand pH 7- 8, and was stable up to 40oC and in the range of pH5- 8. It most rapidly hydrolyzed pNPC6 among various PNPesters.The other contigs were expressed more or less assoluble forms, although no lipolytic activities were detected.As they have many conserved regions with lipase 160-26 aswell as other bacterial lipases throughout their sequence, theyare suggested as true lipase genes.

목차

등록된 정보가 없습니다.

참고문헌 (25)

참고문헌 신청

함께 읽어보면 좋을 논문

논문 유사도에 따라 DBpia 가 추천하는 논문입니다. 함께 보면 좋을 연관 논문을 확인해보세요!

이 논문의 저자 정보

최근 본 자료

전체보기

댓글(0)

0