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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45914

Title: Molecular cloning and biochemical characterization of recombinant laccase from Rigidoporus vinctus.
Authors: Chia-Yu Kuo
Jenq-Kuen Huang
Lisa Wen
Ka-Lai Pang
Chi-Tsai Lin
Contributors: 國立臺灣海洋大學:海洋生物研究所
Keywords: Rigidoporus vinctus
laccase
three-dimension (3-D) structural model
ABTS [2,2'- azinobis- (3- ethylbenzothiozone-6- sulphonic acid)]
Date: 2015
Issue Date: 2018-04-17T06:31:25Z
Publisher: Journal of Marine Science and Technology
Abstract: Abstract: Laccases are multi-copper oxidases that widely distributed in plants and fungi. These enzymes catalyze oxidation of various compounds including phenolics and non-phenolics, and have been used in many industrial processes such as paper industry, biobleaching and bioremediation. A full length cDNA (1767 bp) encoding a putative laccase (Lac) from "Rigidoporus vinctus" was cloned by polymerase chain reaction (PCR). The coding region of RvLac encodes 517 amino acids which contained four conserved putative copper-binding regions. To further characterize the RvLac, the coding region was subcloned into an expression vector pET-20b(+) and transformed into "E. coli" BL21 (DE3) pLysS. Expression of the Lac was induced by IPTG and the recombinant His-tagged Lac was purified by Ni_2+ -nitrilotriacetic acid Sepharose superflow column. The purified enzyme was revealed as a single band on SDS-PAGE with molecular mass of ~57 kDa. Furthermore, the enzyme activity and kinetics were determined by ABTS assay. The Michaelis constant value for ABTS is 0.07 mM. The enzyme has a half-life of 4.6 min at 75℃. The enzyme is active under a pH 2 treatment for 30 min.
Relation: 23(5) pp.827-835
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45914
Appears in Collections:[海洋生物研究所] 期刊論文

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