|dc.contributor.author||Chang Jin Kim||-|
|dc.description.abstract||Laccase 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.title||Properties of laccase purified from nitrogen limited culture of white-rot fungus Coriolus Hirsutus||-|
|dc.title.alternative||Properties of laccase purified from nitrogen limited culture of white-rot fungus Coriolus Hirsutus||-|
|dc.contributor.affiliatedAuthor||Chang Jin Kim||-|
|dc.identifier.bibliographicCitation||Biotechnology Techniques, vol. 12, no. 2, pp. 101-104||-|
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