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The optimum activity of keratinase enzyme was found at pH 8.0 alongside temperature of 40 °C.
Optimum activity of the purified enzyme was obtained at pH 2 and 60 °C with n-propanol as substrate.
Optimum activity of PCL depolymerases was observed at 30 °C and a pH range between 3.5 and 4.5 (Oda et al. 1995).
While an optimum activity of GluDH-BA was observed at a temperature of 50 °C, the enzyme was stable only up to 42 °C.
The optimum activity of AAA at pH > 10 suggests that the reaction mechanism employs Lys84 as the catalytic base to polarize the Ser187 nucleophile in the catalytic triad.
The optimum activity of the 2.5 folds purified esterase was 89.5 U with 20 mM para-nitrophenyl acetate as substrate (50 °C, pH 8.0 and for 30 min), and various metal ions were found to retarde the esterase activity.
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Earlier studies [ 7, 27] reported optimum activities of various WRF LiPs to vary between pH 2 5.
To facilitate optimum activity for the sialidase, influence of various times of incubation and serum volumes was assessed in the assays with GM3 as the substrate.
The enzyme had an activity optimum of 50°C and pH 7, but retained >50% of its optimum activity over a range of temperatures (30 to 55°C) and pH (5.5 to 8) (Figure 3).
To assess the pH at which Na-APR-1wt exhibited optimum activity, 1.0 μg of enzyme was added to 50 mM sodium acetate buffers of differing pH, increasing in half-unit increments from pH 2.0 to 6.0 in the presence of 7-methoxycoumarin-4-acetyl-GKPILFFRLK DNP)- d-Arg-amide (MoCAc-GKPILFFRLK) (Sigma, St. Louis, MO, USA).
The conditions for optimum activity and stability of the PYT was assessed by carrying out studies with respect to temperature and pH.
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