Certain enzymes, such as the Taq polymerase and those found in archaea, exhibit remarkable thermostability, allowing them to withstand extreme temperatures without denaturing. This stability is attributed to multiple factors, including increased residue-to-residue contacts, tighter packing of the enzyme structure, and effective burial of hydrophobic surface areas. For instance, the tungsten-containing aldehyde:ferredoxin oxidoreductase from Pyrococcus furiosus demonstrates these characteristics, contributing to its resilience. However, it is important to note that even extremophiles like P. furiosus have temperature limits, typically around 100°C, and cannot tolerate indefinite increases in heat. Additionally, these enzymes generally prefer neutral pH conditions but can adapt to slight variations.
