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Purification and Characterization of Novel Manganese Peroxidase from Rhizoctonia sp. SYBC-M3
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  • Purification and Characterization of Novel Manganese Peroxidase from Rhizoctonia sp. SYBC-M3
저자명
Cai. Yujie,Wu. Huiguang,Liao. Xiangru,Ding. Yanrui,Sun. Jun,Zhang. Dabing
간행물명
Biotechnology and bioprocess engineering
권/호정보
2010년|15권 6호|pp.1016-1021 (6 pages)
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한국생물공학회
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이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
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기타언어초록

A novel manganese peroxidase of Rhizoctonia sp. SYBC-M3 (R-MnP) was purified by $(NH_4)_2SO_4$ fractionation, DEAE-cellulose-32 column chromatography, and Sephadex G100 column chromatography. The molecular mass of R-MnP was determined to be approximately 40.4 kDa by SDS-PAGE. The optimum temperature and pH for R-MnP were $55^{circ}C$ and 4.5, respectively. R-MnP was highly stability when the temperature was below $50^{circ}C$. R-MnP could retain about 60% of its activity when the pH was between 4 and 6.5. However, R-MnP activity was inhibited by $Fe^{3+}$, $Cu^{2+}$, and $Co^{3+}$ as well as increased by $Zn^{2+}$ and $Ca^{2+}$. R-MnP demonstrated oxidation of DMP, ABTS, veratryl alcohol, and guaiacol. The $K_m$ values of RMnP for $H_2O_2$ and $Mn^{2+}$ were 25.3 and 53.9 ${mu}$mol/L, respectively.