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However, thermophilic enzymes are generally incompatible with thermo-labile substrates, products, and cofactors, since they show the maximal activities at high temperatures.
Singh and Appu Rao [18] claimed that two endo-polygalacturonases from A. niger could achieve their maximal activities at 43 and 45 °C.
We find that temporal patterns of service usages are bound to the typical weekly cycles of humans, yet they show maximal activities at different times.
In this way, we enhance considerably (by forcing the units to add their maximal activities at the same time) the grey level on the zones of local synchronization (Figure 8 E bottom right).
In addition, Xyn11B had maximal activities at 50°C, lower than Xyn11A 60°CC).
The optima of reaction conditions also remained unchanged: both enzymes showed their maximal activities at 50 mM NaCl; 5 mM EDTA; pH 7.0-8.5, and 37°C.
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The optimal temperature for the enzymatic activity of mAP was 37°C and complete thermal inactivation of the enzyme was observed at 65°C within 15 min. mAP was activated by Ca2+ and exhibited maximal activity at pH 9.0.
The purified lipase was active in the temperature range of 20 45°C, with maximal activity at 45°C.
AbnZ3 displayed excellent cold-adapted properties when compared with reported cryophilic endo-arabinanases, like Abnc from P. chrysogenum 31B which was mostly active at 30 to 40°C and remained 55% of maximal activity at 10°C [8].
The enzyme was active in the pH range of 7.5 11.0, with its maximal activity at pH 9.5.
The activity of the recombinant Xyn2 was highest at 60°C and it was active over a broad range of pH (3.0 8.0) with maximal activity at pH 6.0.
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