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
Two endoxylanases from an alkaliphilic bacterium,Bacilus halodurans C-1, were purified 3.8- and 7.9- fold withspecific activities of 9.4 and 19.8 U/mgprotein, respectively.The molecular masses of both purified enzymes were 23 and47 kDa, respectively, and 23 kDa xylanase I (Xyl I) exhibitedan optimum pH at 7.0, whereas 47 kDa xylanase II (Xyl II)showed a broad pH range of 5.0 to 9.0. The temperatureoC and 70oC, respectively.Both were stable in the pH range of 6.0 to 9.0 and 5.0 to 10.0,respectively, and they were stable up to 60oC and 70oC,respectively. The Km and Vmax of Xyl I were 4.33 mg/ml and63.5mol/min/mg, respectively, whereas Xyl II had a Kmvalue of 0.30 mg/ml and Vmax of 210xylanases hydrolyzed xylans from birchwood, oat spelt, andlarchwood. However, they showed diferent modes of action;a series of xylooligosacharides larger than xylotriose werereleased as the major products by Xyl I, whereas xylobiose andxylotriose were the main products by Xyl I. The maximumsynergistic action of the two enzymes on hydrolysis of xylanwas 2.16 with the ratio of Xyl I to Xyl II at 1:9.

목차

등록된 정보가 없습니다.

참고문헌 (24)

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