This book covers the basic structural, thermodynamic and kinetic principles are covered and molecular strategies for the adaptation to high temperatures revealed by structure analysis are delineated. The roles of fluctuations, hydration and internal packing are thoroughly dicussed. Enzymes with a particular industrial importance, the subtilisin-like serine proteases, have been extensively studied by protein engineering. One extensive chapter is devoted to the present state of knowledge concerning structure-function relations and the origin of the their structural stability. Last but not least, computational and experimental approaches for the design of proteins with increased thermal stability based on sequences or 3D structures are present

Thermostable Proteins: Structural Stability and Design provides a comprehensive, updated account of the physical basis of enhanced stability of thermophilic proteins and the design of tailor-made thermostable proteins, paving the way for their possible industrial applications. This book is devoted to understanding the survival mechanisms of thermophilic life forms at the molecular level with an emphasis on design strategies.The review chapters presented in Thermostable Proteins span a wide range of protein thermostability research. Basic structural, thermodynamic, and kinetic principles are explained and molecular strategies for the adaptation to high temperatures are delineated. In addition, this book covers: computing and simulation methods in current and future thermostability research, especially in nonempirical situations, how rigidity theory is used to improve the thermal adaptation of mesophiles Subtilisin-like serine proteases and their significant engineering applications. The state of knowledge concerning structure function relations and the origins of their structural stability. Computational and experimental approaches for the design of proteins with increased thermal stability based on sequences or three-dimensional structures. Understanding the molecular basis of how thermostable and hyperthermostable proteins gain and maintain their stability and biological function at high temperatures remains an important scientific challenge. A more detailed knowledge of protein stability not only deepens our understanding of protein structure but also helps in obtaining insights into processes that drive protein activities folding, unfolding, and misfolding essential to biological function--Provided by publisher.

LIST OF PARTICIPANTS 11 THERMOPHILIC HYDROLYTIC ENZYMES (PROTEINASES, AMYLASES) 17 Thermal Stability of Homologous Neutral Metalloendopeptidases in Thermo philic and Mesophilic Bacteria: Structural Considerations M. K. PANGBURN, P. L. LEVY, K. A. WALSH and H. NEURATH 19 The Structure and Stability of Thermolysin L. H. WEAVER, W. R. KESTER, K. F. TEN EYCK and B. W. MATTHEWS 31 Studies of the Inhibition of Thermolysin J. FEDER, N. AUFDERHEIDE and B. S. WILDI 41 Effect of EDTA on the Conformational Stability of Thermolysin A. FONTANA, E. BOCCU and F. M. VERONESE 55 Role of a Sulfhydryl Group in the Structure and Function of Alkaline Proteases from a Thermophilic Actinomycete K. MIZUSAWA and F. YOSHIDA 61 Partial Characterization of a Thermophilic Actinomycete Rennin S. LAXER, A. PINSKY and B. BARTOOV 67 Amylase Activity and Stability at High and Low Temperature Depending on Calcium and other Divalent Cations W. HEINEN and A. M. LAUWERS 77 Role of Calcium Ion in the Thermostability of a-Amylase Produced from Bacillus stearothermophilus K. YUTAN I 91 THERMOPHILIC DEHYDROGENASES 105 Thermophilic Glyceraldehyde-3-P Dehydrogenase R. E. AMELUNXEN and R. SINGLETON JR. 107 Glyceraldehyde 3-Phosphate Dehydrogenase from an Extreme Thermophile, Thermus aquaticus 121 J. D. HOCKING and J. I. HARRIS Thermal Properties of Glyceraldehyde 3-Phosphate Dehydrogenase from Escherichia coli A. FONTANA, C. GRANDI, E. BOCCU and F. M. VERONESE 135 Comparative Conformational Properties of Thermophilic and Mesophilic 6-Phosphogluconate Dehydrogenase F. M. VERONESE, C. GRANDI, E. BOCCU and A.

This text provides information on thermostability of enzymes. It includes topics such as: structure, stability, isolation and purification of proteins; thermophilic microorganisms; models of enzyme deactivation; and chemical modification and crosslinking for enhancing thermostability for enzymes.

Thermophilic Bacteria is a comprehensive volume that describes all major bacterial groups that can grow above 60-65°C (excluding the Archaea). Over 60 different species of aerobic and anaerobic thermophilic bacteria are covered. Isolation, growth methods, characterization and identification, ecology, metabolism, and enzymology of thermophilic bacteria are examined in detail, and an extensive compilation of recent biotechnological applications and the properties of many thermostable enzymes are also included. Major topics discussed in the book include a general review on thermophilic bacteria and archaea; heterotropic bacilli; the genus Thermus; new and rare genera of aerobic heterophophs, such as Saccharococcus, Rhodothermus, and Scotohermus; aerobic chemolithoautotrophic thermophilic bacteria; obligately anaerobic thermophilic bacteria; and hyperthermophilic Thermotogales and thermophilic phototrophs. Extensive bibliographies are also provided for each chapter. The vast amount of information packed into this one volume makes it essential for all microbiologists, biochemists, molecular biologists, and students interested in the expanding field of thermophilicity. Biotechnologists will find the book useful as a source of information on thermophiles or thermostable enzymes of possible industrial use.

Interest in the study of life in hot environments, both with respect to the inhabiting microorganisms and the enzymes they produce, is currently very high. The biological mechanisms responsible for the resistance to high temperatures are not yet fully understood, whereas thermostability is a highly required feature for industrial applications. In this e-book, the invited authors provide diverse evidence contributing to the understanding of such mechanisms and the unlocking of the biotechnological potential of thermophiles and thermozymes.

All important aspects of thermophilic moulds such as systematics, ecology, physiology and biochemistry, production of extracellular and intracellular enzymes, their role in spoilage of stores products and solid and liquid waste management, and general and molecular genetics have been dealt with comprehensively by experts in this book which covers progress in the field over the last 30 years since the seminal book Thermophilic Fungi published by Cooney and Emerson in 1964. The experts have reviewed extensive literature on all aspects of thermophilic moulds in a very comprehensive manner. This book will be useful for graduates as well as post-graduate students of life sciences, mycology, microbiology and biotechnology, and as a reference book for researchers.