The stabilization of proteins by sucrose.

J. C. Lee, S. N. Timasheff

Research output: Contribution to journalArticlepeer-review

1047 Scopus citations


The interactions between proteins and solvent components have been investigated for the sucrose/water system. Thermodynamic and kinetic measurements of the thermal unfolding of alpha-chymotrypsin, chymotrypsinogen, and ribonuclease were performed as a function of sucrose concentration. The alteration in protein-solvent interactions in the presence of sucrose was also studied by density measurements and analyzed by multicomponent thermodynamic theory. Sucrose does not induce a conformational change in three proteins studied, although it does induce a small change in the circular dichroism spectrum of ribonuclease. The enthalpy of thermal unfolding shows little dependence on the concentration of sucrose, while the apparent activation energy of the unfolding process is increased by the addition of sucrose. The results from the protein-solvent interaction study indicate that sucrose is preferentially excluded from the protein domain, increasing the free energy of the system. Thermodynamically this leads to protein stabilization since the unfolded state of the protein becomes thermodynamically even less favorable in the presence of sucrose. The exclusion of sucrose from the protein domain seems to be related to the higher cohesive force of the sucrose water solvent system since all the experimental observations can be correlated with the effect of sucrose on the surface tension of water.

Original languageEnglish (US)
Pages (from-to)7193-7201
Number of pages9
JournalJournal of Biological Chemistry
Issue number14
StatePublished - Jul 25 1981
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'The stabilization of proteins by sucrose.'. Together they form a unique fingerprint.

Cite this