The effect of pH on the activity of the S. basilisca trypsin was studied using BAPNA as a substrate over a pH range of
7.0–12.0 (Fig. 4c). The purified enzyme was active between pH 8.0 and 11.0, with an optimum around pH 9.5. The relative activities at pH 9.0 and 10.0 were about 94% and 69%, respectively (p < 0.05), of that at pH 9.5. The optimum pH of S. basilisca trypsin was similar to those from other fish species, such as striped seabream (L. mormyrus) (El Hadj-Ali et al., 2009), which showed maximum activity at pH 9.0–10.5 and was higher than those of most described trypsins, which showed maximum activity at pH 8.0.
The effect of pH on the activity of the S. basilisca trypsin was studied using BAPNA as a substrate over a pH range of 7.0–12.0 (Fig. 4c). The purified enzyme was active between pH 8.0 and 11.0, with an optimum around pH 9.5. The relative activities at pH 9.0 and 10.0 were about 94% and 69%, respectively (p < 0.05), of that at pH 9.5. The optimum pH of S. basilisca trypsin was similar to those from other fish species, such as striped seabream (L. mormyrus) (El Hadj-Ali et al., 2009), which showed maximum activity at pH 9.0–10.5 and was higher than those of most described trypsins, which showed maximum activity at pH 8.0.
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