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Effects of pH and Temperature on Recombinant Manganese Peroxidase Production and Stability

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Abstract

The enzyme manganese peroxidase (MnP) is produced by numerous white-rot fungi to overcome biomass recalcitrance caused by lignin. MnP acts directly on lignin and increases access of the woody structure to synergistic wood-degrading enzymes such as cellulases and xylanases. Recombinant MnP (rMnP) can be produced in the yeast Pichia pastoris αMnP1-1 in fed-batch fermentations. The effects of pH and temperature on recombinant manganese peroxidase (rMnP) production by P. pastoris αMnP1-1 were investigated in shake flask and fed-batch fermentations. The optimum pH and temperature for a standardized fed-batch fermentation process for rMnP production in P. pastoris αMnP1-1 were determined to be pH 6 and 30 °C, respectively. P. pastoris αMnP1-1 constitutively expresses the manganese peroxidase (mnp1) complementary DNA from Phanerochaete chrysosporium, and the rMnP has similar kinetic characteristics and pH activity and stability ranges as the wild-type MnP (wtMnP). Cultivation of P. chrysosporium mycelia in stationary flasks for production of heme peroxidases is commonly conducted at low pH (pH 4.2). However, shake flask and fed-batch fermentation experiments with P. pastoris αMnP1-1 demonstrated that rMnP production is highest at pH 6, with rMnP concentrations in the medium declining rapidly at pH less than 5.5, although cell growth rates were similar from pH 4–7. Investigations of the cause of low rMnP production at low pH were consistent with the hypothesis that intracellular proteases are released from dead and lysed yeast cells during the fermentation that are active against rMnP at pH less than 5.5.

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Acknowledgment

This work was supported by the National Science Foundation grants BES-0536128 and BES-0328031.

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Authors and Affiliations

  1. Department of Biomedical and Chemical Engineering, Syracuse University, 121 Link Hall, Syracuse, NY, 13244-1240, USA

    Fei Jiang & Puapong Kongsaeree

  2. School of Chemical, Biological, and Environmental Engineering, Oregon State University, 102 Gleeson Hall, Corvallis, OR, 97331-2701, USA

    Karl Schilke, Curtis Lajoie & Christine Kelly

  3. Cell Genesys, Inc., 500 Forbes Boulevard, South San Francisco, CA, 94080, USA

    Fei Jiang

  4. G C Hanford MFG Company, 304 Oneida St., Syracuse, NY, 13201, USA

    Puapong Kongsaeree

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  1. Fei Jiang
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  2. Puapong Kongsaeree
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  3. Karl Schilke
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  4. Curtis Lajoie
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  5. Christine Kelly
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Correspondence to Christine Kelly.

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Jiang, F., Kongsaeree, P., Schilke, K. et al. Effects of pH and Temperature on Recombinant Manganese Peroxidase Production and Stability. Appl Biochem Biotechnol 146, 15–27 (2008). https://doi.org/10.1007/s12010-007-8039-5

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  • DOI: https://doi.org/10.1007/s12010-007-8039-5

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