The thermodynamics and extra-thermodynamics of Bacillus subtilis α-amylase in five kinds of chromatographic systems were studied by determining their adsorption equilibrium constant K SL , enthalpy change, entropy change, free energy change and compensation temperature under different temperature areas. The results showed that on an RP-C 18 reversed-phase medium, a Zn-chelated Sepharose fast-flow affinity medium and a WCX-1 cation-exchange medium, their ln K SL separately linearly changed with the reciprocal of absolute temperatures under two different temperature ranges of 13-30 and 30-50 ℃; and on PEG-400 and modified PEG-400 hydrophobic media, their ln K SL separately linearly decreased with the reciprocal of absolute temperatures under the temperature areas of 13-40 and 13-30 ℃, while when the temperatures were separately over 40 and 30 ℃, they violently decreased with the reciprocal of absolute temperatures. Through studying the relations among the enthalpy change, entropy change, free energy change and the conformational change of α-amylase under the different temperature areas, it was found that on the RP-C 18 reversed-phase medium and Zn-chelated Sepharose fast-flow affinity medium under the temperature range of 30-50 ℃ and on the WCX-1 cation-exchange medium under the temperature range of 13-30 ℃, their adsorption procedures were driven by both the enthalpy change and the entropy change; while on the Zn-chelated Sepharose fast-flow affinity medium under the temperature range of 13-30 ℃, on the WCX-1 cation-exchange medium under the temperature range of 30-50 ℃ and on the PEG-400 and modified PEG-400 hydrophobic media under the temperature range of 13-65 ℃, their adsorption procedures were driven only by the entropy change. Finally, by comparing the compensation temperatures of α-amylase in these chromatographic systems each other, it was further found that their enthalpy changes could be compensated only with their entropy changes rising from their conformational change.