The moderate stability of enzymes is one of the main drawbacks that hinder general
implementation of these interesting biocatalysts at industrial scale. An especially complex …

The discovery of extremophiles has drastically changed our understanding towards the
diversity of life itself and the conditions under which it can be sustained. Extremophiles have …

Motivation Understanding the molecular mechanisms of thermal stability is a challenge in
protein biology. Indeed, knowing the temperature at which proteins are stable has important …

Motivation Thermal properties of proteins are of great importance for a number of theoretical
and practical implications. Predicting the thermal stability of a protein is a difficult and still …

Exploration of microbial pool from extremely diversified ecosystem is significantly important
for various industrial applications. Bacterial communities from extreme habitats including …

Enzymes that are naturally found in thermophilic and hyperthermophilic organisms are
being used as robust biocatalysts in the fine chemical and pharmaceutical industries. They …

In order to understand the thermodynamic and kinetic basis of the intrinsic stability of
proteins from hyperthermophiles, the folding-unfolding reactions of cysteine-free pyrrolidone …

2-Deoxyribose-5-phosphate aldolase catalyzes a reversible aldol condensation of two
aldehydes via formation of a covalent Schiff-base intermediate at the active lysine residue …

The temperature adaptation of pyrrolidone carboxyl peptidase (PCP) from a
hyperthermophile, Pyrococcus furiosus (Pf PCP), was characterized in the context of an …

Phosphopantetheine adenylyltransferase (PPAT) is an essential enzyme in bacteria that
catalyzes the rate-limiting step in coenzyme A (CoA) biosynthesis by transferring an adenylyl …