10.1371/journal.pone.0191621.g003 Julieta B. Carrillo Julieta B. Carrillo Diego F. Gomez-Casati Diego F. Gomez-Casati Mariana Martín Mariana Martín Maria V. Busi Maria V. Busi Kinetic characterization of OsttaDSP. Public Library of Science 2018 starch metabolism exhibits glycogen degradation electrophoretic homogeneity Ostreococcus tauri Ostreococcus tauri Arabidopsis thaliana LSF 2. enzyme forms Prasinophyceae family residue C 162 dephosphorylates amylopectin glucan phosphatases phosphoglucan phosphatase tauri microalgae OsttaDSP Glucan phosphatases gene coding 54.5 kDa starch granule heterologous expression 2018-01-23 18:33:23 Figure https://plos.figshare.com/articles/figure/Kinetic_characterization_of_OsttaDSP_/5815056 <p><b>A) Effect of pH on the activity of recombinant OsttaDSP.</b> Activity was assayed with <i>p</i>NPP (filled triangles/▲) or amylopectin (filled circles/●) as a substrate using 100 mM Sodium Acetate, 50 mMBis-Tris and 50 mM Tris as a buffer. Buffer pH values were adjusted to the values shown in the graphic and used to assay the enzyme. All data are the means ± SD of 3 independent experiments. <b>B) <i>p</i>NPP saturation plot for OsttaDSP determined at pH 7. C) Amylopectin saturation plot for OsttaDSP determined at pH 7.5.</b></p>