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Xylanase MpXyn10A was overexpressed in Aspergillus nidulans and was active against birchwood xylan, presenting an optimum activity at pH 5.8 and 80°C.
The enzyme was active from pH 6 to 11, with an optimum activity at pH 9 and temperature varied from 5 to 40 °C, with an optimum activity at 15 °C, which can be a crucial in some applications (Fenton et al. 2011).
It is noteworthy to mention that virus T1 DNA MTase shows optimum activity at pH 6.9 [44] while the archaebacterial PabI MTase is active at a pH range of 6.0 to 6.7 [45].
The temperature activity profile shows that the crude α-amylase was active at temperatures ranging from 20 to 70°C with an optimum activity at 60°C).
As shown in Figure 5C, FSAΔSK was active over a broad temperature range (20°C to 100°C) and had an optimum activity at 55°C.
It shows optimum activity at 70 °C and pH 10.
The enzyme showed optimum activity at 55 °C and pH 6.5.
The protein LipR5, displayed optimum activity at 50 °C and pH 8.0.
Crude exo-β-d-glucosaminidase was found to have optimum activity at 42 ± 1 °C and pH 5.6.
Instead, ΔN21 has the optimum activity at ∼ 77 °C, with higher activities than the WT enzyme below this temperature.
The purified GlyDH displayed an optimum activity at pH 7.0 7.5 and was the most stable at pH 8.5 9.5.
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