2 edition of Thermostability of enzymes found in the catalog.
Thermostability of enzymes
|Statement||editor: M. N. Gupta.|
|Contributions||Gupta, M. N.|
|The Physical Object|
|Number of Pages||213|
Enzymes synthesized by hyperthermophiles (bacteria and archaea with optimal growth temperatures of > 80 degrees C), also called hyperthermophilic enzymes, are typically thermostable (i.e., resistant to irreversible inactivation at high temperatures) and are optimally active at high by: The tetrameric enzymes were characterized with respect to thermostability, pH and temperature dependence of the pyruvate reduction and the L-lactate oxidation, substrate specificity, saturation.
Manfred T. Reetz, Selected Examples of Directed Evolution of Enzymes with Emphasis on Stereo‐ and Regioselectivity, Substrate Scope, and/or Activity, Directed Evolution of Selective Enzymes Cited by: 2. The implications of the varying DP enzyme thermostability on the selection of malt by brewers to optimally suit different brewing styles and regimens are outlined. The enhanced secretion and improved thermostability of the truncation mutant enzymes make them more suitable than the DM enzyme for industrial processes. INTRODUCTION Pullulanase (EC ), which catalyzes the hydrolysis of α-1,6-glucosidic linkages in pullulan, amylopectin, and the dextrins of amylopectin, is a well-known starch Cited by:
This work highly enhanced the thermostability of AuXyn11A by N-terminus replacement, and further verified, by site-directed mutagenesis, that Cys 5, Pro 9, and His 14 contributed mainly to the improved thermostability. It will provide an effective strategy for improving the thermostabilities of other by: Thermolabile refers to a substance which is subject to destruction, decomposition, or change in response to term is often used to describe biochemical substances.. For example, many bacterial exotoxins are thermolabile and can be easily inactivated by the application of moderate heat. Enzymes are also thermolabile and lose their activity when the temperature rises. Thermostable enzymes have many desirable characteristics such as thermostability, wide range of pH tolerance and resistance to organic solvents, which make them superior for industrial applications. Conclusion: Thermophilic and hyperthermophilic enzymes represent Cited by: 1.
Your attitude is showing
Longman Pocket Companions
Science in history.
First report from the Committee on Welsh Affairs... session 1983-84
History of Commission Street Chapel and Unity Church.
Fiat money inflation in France
Hydrologic analysis of the Mojave River, California
Drugs, pregnancy and childcare
guide to manuscript collections in the history of psychology and related areas
Physiology or medicine, 1996-2000
Summary statistics and graphical comparisons of specific conductance, temperature, and dissolved oxygen data, Buffalo Bayou, Houston, Texas, April 1986-March 1991
SyntaxTextGen not activatedThe crowded and hydrophobic microenvironment pdf created for immobilized enzymes via the thermally-initiated shrinkage of PNIPAM polymers anchored in the nanopores of mesoporous extraordinary microenvironment can greatly enhance both the catalytic efficiency and thermostability of lipases, which provides a new approach for fabricating robust heterogeneous by: Enzymes synthesized by hyperthermophiles (bacteria and archaea with optimal growth temperatures of >80°C), also called hyperthermophilic enzymes, are typically thermostable (i.e., resistant to irreversible inactivation at high temperatures) and are optimally active at high by: Enzyme thermostability is a property of great importance in the era of designed ebook.
While enzymes are capable of catalyzing reactions with exquisite specificity and selectivity, they are often limited by insufficient stability. Improvements in enzyme activity through protein engineering often come at the cost of reduced by: