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Thermal stabilization of fungal β-glucosidase through glutaraldehyde crosslinking

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Summary

The thermal stability of a purifiedAspergillus niger β-glucosidase (EC 3.2.1.21) has been dramatically increased by intramolecular crosslinking with glutaraldehyde at pH 9.0, followed by borohydride reduction. The stabilization has been shown to be due to the formation of a distinct subpopulation of enzyme molecules, the activity of which has a half-life at 65°C of approximately 40 hours, which is some 80 times as long as that of the native enzyme at this temperature.

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Authors and Affiliations

  1. Fermentation Section, Biotechnology Branch Solar Fuels Division, Solar Energy Research Institute, 1617 Cole Blvd., 80401, Golden, CO

    J. O. Baker, K. K. Oh, K. Grohmann & M. E. Himmel

Authors
  1. J. O. Baker
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  2. K. K. Oh
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  3. K. Grohmann
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  4. M. E. Himmel
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Baker, J.O., Oh, K.K., Grohmann, K. et al. Thermal stabilization of fungal β-glucosidase through glutaraldehyde crosslinking. Biotechnol Lett 10, 325–330 (1988). https://doi.org/10.1007/BF01026159

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  • DOI: https://doi.org/10.1007/BF01026159

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