The development of enzymes for industrial applications relies heavily on the use of
microorganisms. The intrinsic properties of microbial enzymes, eg, consistency …

Temperature profoundly influences physiological responses in animals, primarily due to the
effects on biochemical reaction rates. Since physiological responses are often exemplified …

INTRODUCTION Over billions of years, organisms and their enzymes have been evolving
and adapting in response to selection pressures from their environments. In particular …

Background: Proteins from thermophilic organisms usually show high intrinsic thermal
stability but have structures that are very similar to their mesophilic homologues. From …

The tree of life is split into three main branches: eukaryotes, bacteria, and archaea. Our
knowledge of eukaryotic and bacteria cell biology has been built on a foundation of studies …

Electrostatic contributions to the folding free energy of several hyperthermophilic proteins
and their mesophilic homologs are calculated. In all the cases studied, electrostatic …

Thermostability of proteins in general and especially thermophilic proteins has been subject
of a wide variety of studies based on theoretical and experimental investigation …

Thermostability of a protein is a property which cannot be attributed to the presence of a
particular amino acid or to a post synthetic modification. Thermostability seems to be a …

The crystal structure of AFEST, a novel hyper-thermophilic carboxylesterase from the
archaeon Archaeoglobus fulgidus, complexed with a sulphonyl derivative, has been …

The molecular stability of thermophilic and hyperthermophilic enzymes generally reflects the
growth temperatures of the parent organisms. Extracellular enzymes from the …