Table 2.
Substrate specificity of α-glucan phosphorylase from Pyrococcus furiosus in the synthetic and phosphorolytic directions in the presence of glucose-1-phosphate (G-1-P) after 30 min. Percent conversions were calculated as the amount of sugar phosphate remaining in the reaction after incubation at a specified time, divided by the amount of substrate used in the reaction, and then multiplied by 100. The percent G-1-P produced was expressed as percent relative intensity (RI) which was calculated as: (RI of G-1-P from oligosaccharide)/(RI of G-1-P from maltoheptaose) × 100. Substrate concentration was 7 mg ml–1 for glycogen and 7 mM for maltose through maltoheptaose.
Substrate | G-1-P consumed (Synthetic) | G-1-P produced (Phosphorolytic) |
Maltose | 100 | 0 |
Maltotriose | 95 | 35 |
Maltotetraose | 90 | 61 |
Maltopentaose | 86 | 78 |
Maltohexaose | 82 | 85 |
Maltoheptaose | 80 | 100 |
Glycogen | 75 | 64 |