Protein stability at high temperatures.
The enzymology of hyperthermophilic micro-organisms is a growing field. As increasing numbers of novel high-temperature organisms are isolated and made available through culture collections, and, as biomass becomes more readily available, more laboratories will undoubtedly expand their research interests into this area. The prospect of totally novel enzyme systems and of new approaches to the investigation of fundamental molecular properties will continue to stimulate interest in this field. Studies of thermostable enzymes have already provided valuable data on the relationships between protein stability and activity. The subtle molecular mechanisms which have evolved to stabilize these proteins provide the clues needed for the intelligent design of stabilized mesophilic enzymes, an important target where a combination of high activity at 'low' temperatures and resistance to denaturation is required. The current role of hyperthermophilic enzymes in biotechnology is relatively minor, despite these enzymes having a high 'profile'. While early over-enthusiastic predictions that these enzymes would revolutionize biotechnology should be disregarded, it can reasonably be assumed that, where functional and economic criteria are suitable, thermophilic enzymes will be readily incorporated into current and future biotechnology.
Cowan
D A
DA
Department of Biochemistry and Molecular Biology, University College London, U.K.
D001419:Bacteria / Q000201:enzymology; D001426:Bacterial Proteins / Q000737:chemistry; D001709:Biotechnology; D004355:Drug Stability; D004795:Enzyme Stability; D004798:Enzymes / Q000737:chemistry*; D006358:Hot Temperature
D001426:Bacterial Proteins; D004798:Enzymes