| Title | Purification and Characterization of Laccase from the White Rot Fungus Trametes versicolor |
|---|---|
| Author | Moon-Jeong Han, Hyoung-Tae Choi, and Hong-Gyu Song* |
| Address | Division of Biological Sciences, Kangwon National University, Chuncheon 200-701, Republic of Korea |
| Bibliography | Journal of Microbiology, 43(6),555-560, 2005, |
| DOI | |
| Key Words | enzyme purification, laccase, Trametes versicolor, white rot fungus |
| Abstract | Laccase is one of the ligninolytic enzymes of white rot fungus Trametes versicolor 951022, a strain first isolated in Korea. This laccase was purified 209-fold from culture fluid with a yield of 6.2% using ethanol precipitation, DEAE-Sepharose, Phenyl-Sepharose, and Sephadex G-100 chromatography. T. versicolor 951022 excretes a single monomeric laccase showing a high specific activity of 91,443 U/mg for 2,2''-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) as a substrate. The enzyme has a molecular mass of approximately 97 kDa as determined by SDS-PAGE, which is larger than those of other laccases reported. It exhibits high enzyme activity over broad pH and temperature ranges with optimum activity at pH 3.0 and a temperature of 50oC. The Km value of the enzyme for substrate ABTS is 12.8 M and its corresponding Vmax value is 8125.4 U/mg. The specific activity and substrate affinity of this laccase are higher than those of other white rot fungi, therefore, it may be potentially useful for industrial purposes. |
| Download PDF | 555-560.pdf |