Kinetic Properties of Manganese Peroxidase from the Mushroom Stereum ostrea and its Ability to Decolorize Dyes
분야
자연과학 > 생물
저자
( K. Praveen ) , ( K. Y. Usha ) , ( Buddolla Viswanath ) , ( B. Rajasekhar Reddy )
발행기관
한국미생물생명공학회(구 한국산업미생물학회)
간행물정보
Journal of Microbiology and Biotechnology 2012년, 제22권 제11호, 1540~1548페이지(총9페이지)
파일형식
05212085.pdf [무료 PDF 뷰어 다운로드]
  • ※ 본 자료는 참고용 논문으로 수정 및 텍스트 복사가 되지 않습니다.
  • 구매가격
    4,500원
    적립금
    135원 (구매자료 3% 적립)
    이메일 발송  스크랩 하기
    자료 다운로드  네이버 로그인
    영문초록
    Manganese peroxidase (MnP) was isolated from the culture filtrate of the wood log mushroom Stereum ostrea (S. ostrea), grown on Koroljova medium, and then purified by ammonium sulfate [70% (w/v)] fractionation, DEAEcellulose anion exchange chromatography, and Sephadex G-100 column chromatography, with an attainment of 88.6-fold purification and the recovery of 22.8% of initial activity. According to SDS-PAGE the molecular mass of the MnP was 40 kDa. The optimal pH and temperature were found to be 4.5 and 35oC, respectively. The enzyme was stable even after exposure to a pH range of 4.5 to 6.0, and at temperatures of up to 35oC at a pH of 4.5 for 1h. The Km and Vmax values for the substrate phenol red were found to be 8 ?m and 111.14 U/mg of protein, respectively. The MnP also oxidized other substrates such as guaiacol, DMP, and veratryl alcohol. Sodium azide, EDTA, SDS, Cu2+, and Fe2+, at 1-5 mM, strongly inhibited enzyme activity, whereas Ca2+ and Zn2+ increased enzyme activity. The participation of the purified enzyme in the decolorization of dyes suggests that S. ostrea manganese peroxidase could be effectively employed in textile industries.
    오늘 본 자료
    더보기
    • 오늘 본 자료가 없습니다.
    본 학술논문은 한국학술정보㈜ 각 학회간에 저작권 계약이 체결된 것으로 HAPPY학술이 제공하고 있습니다.
    본 저작물을 불법적으로 이용시는 법적인 제재가 가해질 수 있습니다.
    사업자등록번호 220-87-87785 대표.신현웅 주소.서울시 서초구 방배로10길 18, 402호 대표전화.070-8809-9397
    개인정보책임자.박정아 통신판매업신고번호 제2017-서울서초-1765호 이메일 help@reportshop.co.kr
    copyright (c) 2009 happynlife. steel All reserved.