Your browser doesn't support javascript.
loading
Fungal Growth and Manganese Peroxidase Production in a Deep Tray Solid-State Bioreactor, and In Vitro Decolorization of Poly R-478 by MnP.
Zhao, Xinshan; Huang, Xianjun; Yao, Juntao; Zhou, Yue; Jia, Rong.
Afiliación
  • Zhao X; College of Life Science, Anhui University, Hefei 230601, P.R. China.
  • Huang X; College of Life Science, Anhui University, Hefei 230601, P.R. China.
  • Yao J; College of Life Science, Anhui University, Hefei 230601, P.R. China.
  • Zhou Y; College of Life Science, Anhui University, Hefei 230601, P.R. China.
  • Jia R; College of Life Science, Anhui University, Hefei 230601, P.R. China.
J Microbiol Biotechnol ; 25(6): 803-13, 2015 Jun.
Article en En | MEDLINE | ID: mdl-25537723
The growth of Irpex lacteus F17 and manganese peroxidase (MnP) production in a selfdesigned tray bioreactor, operating in solid-state conditions at a laboratory scale, were studied. The bioreactor was divided into three layers by three perforated trays. Agroindustrial residues were used both as the carrier of bound mycelia and as a nutrient medium for the growth of I. lacteus F17. The maximum biomass production in the bioreactor was detected at 60 h of fermentation, which was consistent with the CO2 releasing rate by the fungus. During the stationary phase of fungal growth, the maximum MnP activity was observed, reaching 950 U/l at 84 h. Scanning electron microscopy images clearly showed the growth situation of mycelia on the support matrix. Furthermore, the MnP produced by I. lacteus F17 in the bioreactor was isolated and purified, and the internal peptide sequences were also identified with mass spectrometry. The optimal activity of the enzyme was detected at pH 7 and 25 °C, with a long half-life time of 9 days. In addition, the MnP exhibited significant stability within a broad pH range of 4-7 and at temperature up to 55 °C. Besides this, the MnP showed the ability to decolorize the polymeric model dye Poly R-478 in vitro.
Asunto(s)
Buscar en Google
Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Peroxidasas / Polímeros / Antraquinonas / Reactores Biológicos / Polyporales Idioma: En Revista: J Microbiol Biotechnol Año: 2015 Tipo del documento: Article Pais de publicación: Corea del Sur
Buscar en Google
Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Peroxidasas / Polímeros / Antraquinonas / Reactores Biológicos / Polyporales Idioma: En Revista: J Microbiol Biotechnol Año: 2015 Tipo del documento: Article Pais de publicación: Corea del Sur