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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/27001

Title: A highly stable cambialistic-superoxide dismutase from Antrodia camphorata: expression in yeast and enzyme properties
Authors: Yi-Jen Liau;Lisa Wen;Jei-Fu Shaw;Chi-Tsai Lin
Contributors: NTOU:Institute of Bioscience and Biotechnology
國立臺灣海洋大學:生物科技研究所
Keywords: Mushroom;Antrodia camphorata;Expression;Cambialistic-superoxide dismutase (Mn/Fe-SOD);Yeast
Date: 2007-08-01
Issue Date: 2011-10-21T02:22:15Z
Publisher: Journal of Biotechnology
Abstract: Abstract:A cDNA encoding a putative superoxide dismutase (SOD) was identified in expressed sequence tags of Antrodia camphorata, a medicinal mushroom found only in Taiwan. The deduced protein was aligned with Mn-SODs and Fe-SODs from other organisms, this SOD showed greater homology to Mn-SOD. Functional A. camphorata SOD protein was overexpressed in yeast and purified. The purified enzyme showed two active forms on a 12.5% native PAGE, a dimer and a monomer. The dimeric protein's half-life of deactivation at 80 °C was 7 min, and its thermal inactivation rate constant Kd was 9.87 × 10−2 min−1. The enzyme was stable in a broad pH range from 5–11; in the presence of 0.4 M imidazole and 2% SDS. The atomic absorption spectrometric assay showed that 1.0 atom of manganese/iron (9:1) was present in each SOD subunit. The high stability of the enzyme make it better suited than other cambialistic-SODs for use in cosmetics. The SOD also documents its future utility in developing anti-inflammatory agent and in the treatment of chronic diseases.
Relation: 131(1), pp.84–91
URI: http://ntour.ntou.edu.tw/handle/987654321/27001
Appears in Collections:[生命科學暨生物科技學系] 期刊論文

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