Lysozyme reactivation using immobilized molecular chaperonin GroEL

Abstract

The molecular chaperonin, GroEL, was immobilized to a porous matrix and used to reactivate denatured lysozyme. The maximum reactivation yield was obtained at 37 °C and pH 6–8 and about 90% activity of the denatured lysozyme was restored under the conditions. The coupling density of GroEL had little effect on the chaperoning activity of GroEL up to 48 mg g−1 gel. The immobilized GroEL was reusable, indicating the possibility of using it on a large scale for the refolding of proteins.

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Correspondence to Yan Sun.

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Dong, XY., Yang, H. & Sun, Y. Lysozyme reactivation using immobilized molecular chaperonin GroEL. Biotechnology Techniques 13, 637–641 (1999). https://doi.org/10.1023/A:1008920515993

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  • GroEL
  • immobilization
  • lysozyme
  • reactivation
  • refolding