Properties of laccase purified from nitrogen limited culture of white-rot fungus Coriolus Hirsutus

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dc.contributor.authorShin, Kwang-soo-
dc.contributor.authorChang Jin Kim-
dc.date.accessioned2017-04-19T08:55:29Z-
dc.date.available2017-04-19T08:55:29Z-
dc.date.issued1998-
dc.identifier.issn0951-208X-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/4468-
dc.description.abstractLaccase produced by nitrogen-limited culture of Coriolus hirsutus was purified to electrophoretic homogeneity (133-fold) with an overall yield of 40%. The molecular mass of the enzyme was determined as 82 kDa by SDS-PAGE and 80 kDa using gel filtration. It had a pl of 3.50. With ferulic acid and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonate) (ABTS) as the substrate, the enzyme had optimal activity at pH 4.0 and 2.5, respectively. The enzyme was stable in the range pH 5.5 to 7.0 at 30 °C for 1 h. The enzyme was optimally active at 70 °C and it lost all activity within 15 min at 80 °C. The apparent K(m) value of enzyme toward ABTS was 67 °M and had highest affinity toward sinapinic acid. The enzyme was totally inhibited by 0.01 mM cysteine.-
dc.publisherSpringerko
dc.titleProperties of laccase purified from nitrogen limited culture of white-rot fungus Coriolus Hirsutus-
dc.title.alternativeProperties of laccase purified from nitrogen limited culture of white-rot fungus Coriolus Hirsutus-
dc.typeArticle-
dc.citation.titleBiotechnology Techniques-
dc.citation.number2-
dc.citation.endPage104-
dc.citation.startPage101-
dc.citation.volume12-
dc.contributor.affiliatedAuthorChang Jin Kim-
dc.contributor.alternativeName신광수-
dc.contributor.alternativeName김창진-
dc.identifier.bibliographicCitationBiotechnology Techniques, vol. 12, no. 2, pp. 101-104-
dc.identifier.doi10.1023/A:1008824130769-
dc.subject.keywordCoriolus-
dc.subject.keywordFungi-
dc.subject.localCoriolus-
dc.subject.localFungi-
dc.subject.localfungi-
dc.description.journalClassN-
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