A thioredoxin from hyperthermophile, Methanococcus jannashii (MjTRX) was characterized by use of the differential scanning calorimetry to understand the mechanisms of thermodynamic stability. MjTRX has an unfolding transition temperature of 116.5$^{circ}C$, although the maximum free energy of the unfolding (9.9 Kcal/mol) is similar to that of E. coli thioredoxin (ETRX, 9.0 Kcal/mol). However, the temperature of maximum stability is higher than ETRX by 20$^{circ}C$, indicating that the unfolding transition temperature increased by shifting the temperature of maximum stability. MjTRX has lower enthalpy and entropy of the unfolding compared to ETRX maintaining a similar free energy of the unfolding. From the structure and the thermodynamic parameters of MjTRX, we showed that the unfolding transition temperature of MjTRX is increased due to the decreased entropy of the unfolding. Decreasing the unfolded state entropy and increasing the folded state entropy can decrease the entropy of the unfolding. In the case of MjTRX, the increased number of proline residues decreased the unfolded state entropy and the increased enthalpy in the folded state increased the folded state entropy.