DBF (DISULFIDE BOND-FORMING) ENZYME FROM THE HYPERTHERMOPHILIC ARCHAEBACTERIUM SULFOLOBUS-SOLFATARICUS BEHAVES LIKE A MOLECULAR CHAPERONE

DBF enzyme from the hyperthermophilic archaebacterium Sulfolobus solfa taricus greatly enhances the refolding at 30 degrees C of denatured an d reduced bovine pancreatic ribonuclease (Guagliardi et al., 1992). He re 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 comple te amino acid sequence of DBF. The role of molecular chaperones from t hermophilic microorganisms in applied biocatalysis is discussed.