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Influence of high temperature and ethanol on thermostable lignocellulolytic enzymes

  • Bioenergy/Biofuels/Biochemicals
  • Published:
Journal of Industrial Microbiology & Biotechnology

Abstract

Lignocellulolytic enzymes are among the most costly part in production of bioethanol. Therefore, recycling of enzymes is interesting as a concept for reduction of process costs. However, stability of the enzymes during the process is critical. In this work, focus has been on investigating the influence of temperature and ethanol on enzyme activity and stability in the distillation step, where most enzymes are inactivated due to high temperatures. Two enzyme mixtures, a mesophilic and a thermostable mixture, were exposed to typical process conditions [temperatures from 55 to 65 °C and up to 5 % ethanol (w/v)] followed by specific enzyme activity analyses and SDS-PAGE. The thermostable and mesophilic mixture remained active at up to 65 and 55 °C, respectively. When the enzyme mixtures reached their maximum temperature limit, ethanol had a remarkable influence on enzyme activity, e.g., the more ethanol, the faster the inactivation. The reason could be the hydrophobic interaction of ethanol on the tertiary structure of the enzyme protein. The thermostable mixture was more tolerant to temperature and ethanol and could therefore be a potential candidate for recycling after distillation.

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Acknowledgments

This research was financed by the EU project HYPE, grant agreement no. 213139. The authors thank Roal Oy and VTT (Finland) for providing thermostable enzymes and Novozymes (Denmark) for providing Celluclast and Novozym188.

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  1. Faculty of Science, University of Copenhagen, Rolighedsvej 23, 1958, Frederiksberg C, Denmark

    Pernille Anastasia Skovgaard & Henning Jørgensen

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  1. Pernille Anastasia Skovgaard
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  2. Henning Jørgensen
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Correspondence to Henning Jørgensen.

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Skovgaard, P.A., Jørgensen, H. Influence of high temperature and ethanol on thermostable lignocellulolytic enzymes. J Ind Microbiol Biotechnol 40, 447–456 (2013). https://doi.org/10.1007/s10295-013-1248-8

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  • DOI: https://doi.org/10.1007/s10295-013-1248-8

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