Final answer:
Enzymes from warm-adapted organisms are more thermally stable due to various structural adaptations, allowing them to function at high temperatures. These properties are utilized in industrial applications such as PCR and hot-water detergents.
Step-by-step explanation:
Enzymes from warm-adapted organisms, such as thermophiles and hyperthermophiles, tend to be more thermally stable than those from organisms adapted to moderate temperatures (mesophiles). This thermal stability is evidenced by structural adaptations that allow these enzymes to function optimally at higher temperatures. For example, thermophilic enzymes may possess a higher ratio of saturated lipids in their membranes to reduce fluidity, a greater proportion of guanine-cytosine base pairs in their DNA, which offers more robust hydrogen bonding, and key amino acid substitutions that strengthen enzyme folding and resistance to denaturation.
Enzymes such as Taq polymerase are adapted to operate at temperatures nearing or even exceeding 100°C. In contrast, enzymes in human pathogens typically require temperatures close to human body temperature (37°C) to function effectively. The thermal stability of enzymes from thermophiles is harnessed in industrial applications, such as in the polymerase chain reaction (PCR) and in hot-water detergents, where their activity at high temperatures is beneficial.