Cold-adapted (psychrophilic) enzymes have intrinsically high activities at the expense of low stabilities due to their flexible structures. Their higher thermolability limits their applications under numerous industrial conditions that require the process to be carried out at higher temperatures for efficient catalysis. Therefore, for effective utilization, cold-adapted enzymes need to be improved in such a way that enhances their stability with an increase or retention of their activity. This chapter discusses the thermodynamic aspects of improvement of catalytic properties and presents a unified strategy that aims at simultaneously improving the activity and stability of cold-adapted enzymes by employing not a single but a combination of approaches that include genetic and chemical modifications, immobilization, nonaqueous solvents, and additives. This concept aims to take cold-adapted enzymes a step further from current potential to cost-effective tangible commercial applications.