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© Research
Publication : European journal of biochemistry

Inclusion bodies of the thermophilic endoglucanase D from Clostridium thermocellum are made of native enzyme that resists 8 M urea

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in European journal of biochemistry - 01 Apr 1992

Chaffotte AF, Guillou Y, Goldberg ME

Link to Pubmed [PMID] – 1555596

Eur. J. Biochem. 1992 Apr;205(1):369-73

Endoglucanase D from Clostridium thermocellum was purified from inclusion bodies formed upon its overproduction in Escherichia coli, using 5 M urea as a solubilizing solution. We examined the effects of denaturing agents upon the stability of the pure soluble enzyme as a function of the temperature. At room temperature, guanidinium chloride induces an irreversible denaturation. By comparison, we observed no structural or functional effects at room temperature using high concentrations of urea as denaturing agent. The irreversible denaturation process observed with guanidinium chloride also occurs with urea but only at elevated temperature (greater than or equal to 60 degrees C); in 6 M urea, the activation energy of the denaturation reaction is decreased by a factor of only 1.8. We interpret the high resistance of this protein to urea as reflecting a reduced flexibility of its structure at normal temperatures which should be correlated to the thermophilic origin of this protein.

https://www.ncbi.nlm.nih.gov/pubmed/1555596