DBF (Disulfide Bond Forming) Enzyme from the Hyperthermophilic ArchaebacteriumSulfolobus SolfataricusBehaves Like a Molecular Chaperone

DBF enzyme from the hyperthermophilic archaebacterium Sulfolobus solfataricus greatly enhances the refolding at 30 degrees C of denatured and reduced bovine pancreatic ribonuclease (Guagliardi et al., 1992). Here we show that DBF behaves like a molecular chaperone: it affects in an ATP-dependent manner the in vitro refolding at 50 degrees C of two thermostable dehydrogenases, an alcohol dehydrogenase and a glutamate dehydrogenase from S. solfataricus. This paper also reports the complete amino acid sequence of DBF. The role of molecular chaperones from thermophilic microorganisms in applied biocatalysis is discussed.