Download Biocatalysis at Extreme Temperatures. Enzyme Systems Near by Michael W. W. Adams, Robert M. Kelly PDF

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, tremendous thermophilic organisms / Michael W.W. Adams ... [et al.] --Characterization of enzymes from high-temperature micro organism / Robert M. Kelly ... [et al.] --
Thermally sturdy urease from thermophilic micro organism / Kenneth Runnion, Joan Combie, and Michael Williamson --
breathing electron-transport elements 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 concepts 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 ways to modeling and studying 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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Extra info for Biocatalysis at Extreme Temperatures. Enzyme Systems Near and Above 100 °C

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Later results on optimization revealed addi­ tional increases in biomass production when casein was substituted for peptone. This increase might perhaps be synergistic with nitrogen limitation as previously dis­ cussed toward urease stimulation or biosynthesis. W. ; Washington.

Chapter 4 Thermally Stable Urease from Thermophilic Bacteria 1 1 2 Kenneth Runnion , Joan Combie , and Michael Williamson 1 J. K. S. ch004 2 Thermophilic microorganisms producing heat stable ureases have been isolatedfromthe thermal waters of Yellowstone National Park in Wyoming. Conditions for optimized laboratory culturing were investigated as a means to achieve an economical methodology for the commercial production of an alternative stable enzyme used in clinical, industrial and environmental enzyme-based assays.

However, because it is a very large, monomeric enzyme with a large hydrophobic core, techniques for its characterization involving protein unfolding may not be useful. ; ACS Symposium Series; American Chemical Society: Washington, DC, 1992. 58 TEMP deg C Figure 2. Initial DSC scan of the α-glucosidase from P. furiosus. 0. The ordinate is heat capacity expressed in units of mcal-g"- K . 1 _1 2500 Note: Curves are displaced vertically by 500 mcal/g Κ for convenience of presentation 1 M GuHCl 1500 -1000 45 50 55 60 65 70 75 80 85 90 95 100 105 Temperature (°C) Figure 3.

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