Stabilization of multimeric enzymes: Strategies to prevent subunit dissociation
R Fernandez-Lafuente - Enzyme and microbial technology, 2009 - Elsevier
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 …
implementation of these interesting biocatalysts at industrial scale. An especially complex …
Recent progress towards the application of hyperthermophiles and their enzymes
H Atomi - Current opinion in chemical biology, 2005 - Elsevier
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 …
diversity of life itself and the conditions under which it can be sustained. Extremophiles have …
Insights on protein thermal stability: a graph representation of molecular interactions
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 …
protein biology. Indeed, knowing the temperature at which proteins are stable has important …
[PDF][PDF] Thermometer: a webserver to predict protein thermal stability
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 …
and practical implications. Predicting the thermal stability of a protein is a difficult and still …
Calcium alginate matrix increases the stability and recycling capability of immobilized endo-β-1,4-xylanase from Geobacillus stearothermophilus KIBGE-IB29
Exploration of microbial pool from extremely diversified ecosystem is significantly important
for various industrial applications. Bacterial communities from extreme habitats including …
for various industrial applications. Bacterial communities from extreme habitats including …
Natural methods of protein stabilization: thermostable biocatalysts
JA Littlechild, J Guy, S Connelly, L Mallett… - Biochemical Society …, 2007 - portlandpress.com
Enzymes that are naturally found in thermophilic and hyperthermophilic organisms are
being used as robust biocatalysts in the fine chemical and pharmaceutical industries. They …
being used as robust biocatalysts in the fine chemical and pharmaceutical industries. They …
The unusually slow relaxation kinetics of the folding-unfolding of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus
JK Kaushik, K Ogasahara, K Yutani - Journal of molecular biology, 2002 - Elsevier
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 …
proteins from hyperthermophiles, the folding-unfolding reactions of cysteine-free pyrrolidone …
Structure of aldolase from Thermus thermophilus HB8 showing the contribution of oligomeric state to thermostability
NK Lokanath, I Shiromizu, N Ohshima… - … Section D: Biological …, 2004 - journals.iucr.org
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 …
aldehydes via formation of a covalent Schiff-base intermediate at the active lysine residue …
Thermal stability of pyrrolidone carboxyl peptidases from the hyperthermophilic Archaeon, Pyrococcus furiosus
K Ogasahara, NN Khechinashvili… - European Journal of …, 2001 - Wiley Online Library
The temperature adaptation of pyrrolidone carboxyl peptidase (PCP) from a
hyperthermophile, Pyrococcus furiosus (Pf PCP), was characterized in the context of an …
hyperthermophile, Pyrococcus furiosus (Pf PCP), was characterized in the context of an …
Structure and implications for the thermal stability of phosphopantetheine adenylyltransferase from Thermus thermophilus
H Takahashi, E Inagaki, Y Fujimoto… - … Section D: Biological …, 2004 - journals.iucr.org
Phosphopantetheine adenylyltransferase (PPAT) is an essential enzyme in bacteria that
catalyzes the rate-limiting step in coenzyme A (CoA) biosynthesis by transferring an adenylyl …
catalyzes the rate-limiting step in coenzyme A (CoA) biosynthesis by transferring an adenylyl …