PnbA2 remains stable at temperatures ranging from 25-40°C, and stability of the enzyme decreases gradually above 40°C. PnbA2 activity gradually decreases with temperature increasing, the enzyme retain a part of its activity at 55°C
LIP4 is stable at temperatures below 45°C and loses about 36% of its activity when incubated for 60 min at 50°C, while the enzyme is completely inactivated at 80°C. The half-life of the enzyme is 103 min at 50°C, 36 min at 55°C, and 9 min at 60°C without any additive
the wild-type enzyme has a melting temperature (Tm) of 47°C and an unfolding transition at 45°C, while the double mutant NaM1H2 melts at 63°C and unfolds at 60°C. The mutants NaM1N96S and NaM1F210L show thermal unfolding at 50°C and have a melting temperature of 52°C, and lose all secondary structures at 70°C
at 60 and 65°C, the enzyme is stable for half an hour; whereas incubation at 70°C for half an h leads to a 50% loss of activity. At 65°C, the stability of carboxylesterase decreases to 70% of the total. After 70°C, a sharp decline in the enzyme activity is observed
the enzyme is stable for 42 h at 60°C, however an important decrease in stability is observed at 70°C, where the enzyme retains 63% of its initial activity, down to 43% at 75°C and further to 75% at 80°C after 10 min
bovine serum albumin exhibits a 133fold increase in its turnover number toward 4-nitrophenyl palmitate from 70 to 150°C, at 160°C a slight decrease in esterase activity is observed
isozymr Ces3-1 retains maximum catalytic activity when incubated for 15 min up to 70°C, after which the esterase is rapidly inactivated displaying no activity after treatment at 74°C for 15 min
carboxylesterase activities are stable for 1 h of incubation at 25°C for all tissues, although a significant loss of CbE activity to 4-nitrophenyl valerate (20-67% decrease) is observed for all tissue except anterior intestine when the incubation period is prolonged up to 24 h
the enzyme retains 80% of its activity after incubation at 30°C to 70°C for 30 min and loses 50% of its activity after incubation for 15 min at 80°C, the enzyme is relatively stable below 60°C, while the inactivation rate increases dramatically above this temperature
purified recombinant enzyme, at 30°C and 40°C, lipolytic activity is conserved after 30 and 20 min, respectively. When the enzyme is preincubated around the physiological temperature at 50-60°C for 30 min, lipolytic activity is increased by 80%, it is diminished by 50% at 70°C and completely lost at 80°C after 10 min
the enzyme is inactivated at 50°C in biphasic kinetics where the t1/2 value of the fast phase of inactivation is less than 1 min. The half-life of mutant enzyme N248A/P256Q/E257G/S283F exceeds 120 min
purified recombinant wild-type enzyme lose of 50% activity after 25 min, mutant N96S loses 50% activity after 20 min, mutant F210L loses 80% after 20 min, while mutant NaM1H2 (N96S/F210L) is completely stable for 25 min
purified recombinant wild-type enzyme, inactivation within 5 min. Purified recombinant mutant NaM1H2 is completely stable for 60 min, and shows 150% activity after 15 min
a 60% transient increase in activity is detected when the enzyme is incubated at 90°C for between 10 and 25 min. The activity then rapidly returns to the original level, and is stable for 120 min
half-life of recombinant enzyme expressed in Sulfolobus solfataricus: 16 h. Recombinant enzyme expressed in Escherichia coli loses about 50% of its activity
between 20°C and 60°C a small but significant decrease of the beta-sheet bands occurrs, indicating a partial loss of beta-sheets. This suggests the presence of a temperature-sensitive beta-sheet. The increase in temperature from 60°C to 98°C induces a decrease of alpha-helix and beta-sheet bands which are still detected at 98°C indicating that at this temperature some secondary structure elements of the protein remain intact. The conformational dynamics of the esterase investigated by frequency-domain fluorometry and anisotropy decays show that the temperature affects the protein conformational dynamics
between 20°C and 60°C a small but significant decrease of the beta-sheet bands occurrs, indicating a partial loss of beta-sheets. This suggests the presence of a temperature-sensitive beta-sheet. The increase in temperature from 60°C to 98°C induces a decrease of alpha-helix and beta-sheet bands which are still detected at 98°C indicating that at this temperature some secondary structure elements of the protein remain intact. The conformational dynamics of the esterase investigated by frequency-domain fluorometry and anisotropy decays show that the temperature affects the protein conformational dynamics
circular dichroism results indicated that rP186_1588 shows slight structure alteration from 60 to 90 °C. Comparative molecular simulations at different temperatures (27°C, 80°C, 100°C and 200°C) reveal that its thermostability is associated with its conformational rigidity