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. 2024 May 18;22(5):230. doi: 10.3390/md22050230

Figure 2.

Figure 2

Heterologous expression and biochemical characterization of the alginate lyase AlyC7. (A) SDS-PAGE analysis of the purified recombinant alginate lyase AlyC7. The arrow indicates the AlyC7 band. (B) Substrate specificity of AlyC7. SA, sodium alginate. (C) The effect of temperature on AlyC7 activity. (D) The effect of pH on AlyC7 activity. (E) The effect of NaCl concentration on AlyC7 activity. The data shown in the graphs (CE) are from triplicate experiments (mean ± standard deviation [S.D.]). (F) Analysis of the minimal substrate of AlyC7. Commercial saturated mannuronate oligosaccharides were used as a control. (G) Time-course degradation of AlyC7 towards sodium alginate. DP, degree of polymerization. DP1 to DP6 represent mono-, di-, tri-, tetra-, penta- and hexa-saccharide, respectively. Figures in (F,G) are representatives of triplicate experiments.