By Michael W. W. Adams, Robert M. Kelly
content material: Biocatalysis close to and above 100°C : an outline / Michael W.W. Adams and Robert M. Kelly --
Metabolic enzymes from sulfur-dependent, super thermophilic organisms / Michael W.W. Adams ... [et al.] --Characterization of enzymes from high-temperature micro organism / Robert M. Kelly ... [et al.] --
Thermally solid urease from thermophilic micro organism / Kenneth Runnion, Joan Combie, and Michael Williamson --
respiration electron-transport parts in hyperthermophilic micro organism / R.J. Maier, L. Black, T. Pihl, and B. Schulman --
Key enzymes within the fundamental nitrogen metabolism of a hyperthermophile / Frank T. Robb .. [et al.] --
Biocatalysis in natural media / Don A. Cowan and Adrian R. Plant --
strain dependence of enzyme catalysis / Peter C. Michels and Douglass S. Clark --
Thermodynamic thoughts for protein layout : elevated temperature balance / Martin Straume, Kenneth P. Murphy, and Ernesto Freire --
balance of extreme temperature enzymes : improvement and checking out of a brand new predictive version / Bruce E. Dale and John P. McBennett --
Computational techniques to modeling and reading thermostability in proteins / John E. Wampler ... [et al.] --
DNA-binding proteins and genome topology in thermophilic prokaryotes / D.R. Musgrave ... [et al.] --
purposes of thermostable DNA polymerases in molecular biology / E.J. Mather.
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Additional info for Biocatalysis at Extreme Temperatures. Enzyme Systems Near and Above 100 °C
RUNNION ET AL. Thermally Stable Urease from Thermophilic Bacteria ing of a conjugate to a complimentary antigen. Microbial ureases, as opposed to Jack bean urease which has a relative molecular mass (Mr) of 590K (7, 8), are considerably smaller having been reported in the range of 125K to 380K (7). Commercially available urease is obtained predominantly from jack beans (Canavalia ensiformis). Manufacturers suggest storage in a dry state at 4 to -20°C for stability. Such low temperatures are not practical for home health care kits, diagnostic kits in physician offices and health clinics and fieldable kits for monitoring ecotoxicity and pollution.
One of the most attractive approaches to addressing enzyme structure and function at elevated temperatures is to choose an enzyme which has many well-characterized counterparts from less thermophilic sources. If many prevailing hypotheses are correct, it may be that a relatively small number of changes in amino acid sequence can impart significant thermostability to a particular enzyme. This might be sorted out if a series of homologous enzymes, with increasing thermostability, could be examined.
Woesii as compared to mesophilic counterparts leads to a similar conclusion concerning the role of rigidity in thermostability (3). The P. furiosus a-glucosidase also exhibits considerable stability when pre-incubated at 98°C for 30 minutes in the presence of several common protein denaturants (see Table V). Maintenance of activity in the presence of high levels of DTT most likely indicates that disulfide linkages are not important contributors to the stability of this protein. In addition, SDS does not completely denature the enzyme, and so, as discussed above, caution must be used in the interpretation of SDS-PAGE results.