EC Number   |
Substrates |
Organism  |
Products |
Reversibility |
|---|
    3.2.1.41 | 3 glycogen + H2O |
- |
Anaerobranca gottschalkii |
4 maltotriose |
- |
? |
| 3.2.1.41 | amylopectin + H2O |
- |
Anaerobranca gottschalkii |
maltotriose |
- |
? |
| 3.2.1.41 | more |
no substrate: amylose |
Anaerobranca gottschalkii |
? |
- |
? |
| 3.2.1.41 | pullulan + H2O |
- |
Anaerobranca gottschalkii |
maltotriose + ? |
final product |
? |
| 3.2.1.41 | starch + H2O |
- |
Anaerobranca gottschalkii |
maltotriose + ? |
- |
? |
| 3.2.1.41 | pullulan + H2O |
soluble enzyme is highly reactive towards pullulan but was unable to degrade short branches in starch |
Anoxybacillus ayderensis |
maltotriose + ? |
- |
? |
| 3.2.1.41 | starch + H2O |
following immobilization through covalent attachment to three epoxides (ReliZyme EP403/M, ImmobeadIB-150P, and Immobead IB-150A) and an amino-epoxide (ReliZyme HFA403/M), all PulASK derivatives are active on both short and long branches in starch producing reducing sugars (predominantly maltotriose) and oligosaccharides (chain lenght G8 and higher), respectively, a feature that is absent in the free enzyme. Individual or coimmobilization causes changes in the product specificity, presumably due to changes in the enzyme binding pocket caused by the influence of carrier surface properties (hydrophobicor hydrophilic) and the lengths of the spacer arms |
Anoxybacillus ayderensis |
maltotriose + oligosaccharides |
- |
? |
| 3.2.1.41 | pullulan + H2O |
soluble enzyme is highly reactive towards pullulan but was unable to degrade short branches in starch |
Anoxybacillus ayderensis DSM 28779 |
maltotriose + ? |
- |
? |
| 3.2.1.41 | starch + H2O |
following immobilization through covalent attachment to three epoxides (ReliZyme EP403/M, ImmobeadIB-150P, and Immobead IB-150A) and an amino-epoxide (ReliZyme HFA403/M), all PulASK derivatives are active on both short and long branches in starch producing reducing sugars (predominantly maltotriose) and oligosaccharides (chain lenght G8 and higher), respectively, a feature that is absent in the free enzyme. Individual or coimmobilization causes changes in the product specificity, presumably due to changes in the enzyme binding pocket caused by the influence of carrier surface properties (hydrophobicor hydrophilic) and the lengths of the spacer arms |
Anoxybacillus ayderensis DSM 28779 |
maltotriose + oligosaccharides |
- |
? |
| 3.2.1.41 | more |
the enzyme preferably debranches long branches at alpha-1,6 glycosidic bonds of starch, producing amylose, linear or branched oligosaccharides, but is nonreactive against short branches. In addition, the enzyme acts as limit dextrinase, reaction of EC 3.2.1.142, releasing maltotriose, maltotetraose and maltopentaose from limit dextrin |
Anoxybacillus sp. |
? |
- |
? |
