Trehalose at 10-30% (w/w) greatly stabilized bovine serum albumin (BSA) against thermal denaturation. The highest stabilization was reached in 30% trehalose at 65 degrees C, when the protein's half life was increased from 72 to 335 min. A kinetic analysis based on the Lumry-Eyring mechanism of inactivation showed that BSA denaturation can be described by a first-order rate expression with an apparent activation energy ranging from 238.1 to 246.4 kJ mol(-1).