Figures & data
Fig. 1. Electrophoretic analysis of PYG.
Notes: A: BN-PAGE of PYG. Lane M, marker proteins; lanes 1 and 2, PYG (4 μg protein for each lane) visualized by protein staining and activity staining, respectively. B: SDS-PAGE of PYG. Lane M, marker proteins; lane 1, 5.5 μg PYG.
Fig. 2. MALDI-TOF-MS analysis of PYG tryptic peptides.
Notes: A: MALDI-TOF-MS spectra of tryptic peptides obtained from 51-kDa component. B: MALDI-TOF-MS spectra of tryptic peptides obtained from 40-kDa component.
Fig. 3. Effect of various salts on enzyme activity.
Notes: Maltose hydrolysis rates measured in the presence of 0–400 mM MgCl2 (■), CaCl2 (□), KCl (●), NaCl (○), and MgSO4 (▲) represent in panel at left. Panel at right shows an enlarged view at low concentration of salts (0–5 mM).
Table 1. PYG purification summary.
Fig. 4. Effect of NaCl on the pH–activity profile (A), the pH–stability (B), the temperature–activity profile (C), and the thermal stability (D) of PYG in the absence (○) and presence (●) of 300 mM NaCl.
Notes: A: Enzyme activity was measured at various pH values and 37 °C. B: Enzyme was incubated at various pH values at 4 °C for 24 h, and the residual activity was measured at pH 5.0 and 37 °C. C: Enzyme activity was measured at the indicated temperature and pH 5.0. D: Enzyme was incubated at various temperatures at pH 5.0 for 15 min, and residual activity was measured at pH 5.0 and 37 °C.
