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Lysozyme reactivation using immobilized molecular chaperonin GroEL

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Biotechnology Techniques

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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References

  • Altamirano MM, Golbik R, Zahn R, Buckle AM, Fersht AR (1997) Refolding chromatography with immobilized mini-chaperones. Proc. Natl. Acad. Sci. USA 94: 3576-3578.

    Google Scholar 

  • Fisher MT (1992) Promotion of the in vitro renaturation of dodecametric glutamine synthetase from Escherichia coli in the presence of GroEL (chaperonin-60) and ATP. Biochemistry 31: 3955-3963.

    Google Scholar 

  • Guise AD, Chaudhuri JB (1998) Recovery and reuse of the molecular chaperone GroEL for in vitro protein refolding. Biotechnol. Prog. 14: 343-346.

    Google Scholar 

  • Hartl F-U (1996) Molecular chaperones in cellular protein folding. Nature 381: 571-580.

    Google Scholar 

  • Imoto T, Yagishita K (1971) A simple activity measurement of lysozyme. Agric. Biol. Chem. 35: 1154-1156.

    Google Scholar 

  • Ishii Y, Teshima T, Kondo A, Murakami K, Sonezaki S, Ogawa H, Kato Y, Fukuda H (1997) Operation conditions of enzyme refolding by chaperonin and recycle system using ultrafiltration. Chem. Eng. J. 65: 151-157.

    Google Scholar 

  • Jenkins AJ, March JB, Oliver IR, Masters M (1986) DNA fragment containing the groE genes can suppress mutations in Escherichia coli dnaA genes. Mol. Gen. Genet. 202: 446-454.

    Google Scholar 

  • Mendoza JA, Rogers E, Lorimer GH, Horowitz PM (1991) Chaperonins facilitate the in vitro folding of monometric mitochondrial rhodanase. J. Biol. Chem. 266: 13044-13049.

    Google Scholar 

  • Sadana A (1995) Protein refolding and inactivation during bioseparation: Bopprocessing implications. Biotechnol. Bioeng. 48: 481-489.

    Google Scholar 

  • Teshima T, Kondo A, Fukuda H (1997) Reactivation of thermally inactivated enzymes by free and immobilized chaperonin GroEL/ES. Appl. Microbiol. Biotechnol. 48: 41-46.

    Google Scholar 

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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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  • DOI: https://doi.org/10.1023/A:1008920515993

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