EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
3.2.1.41 | starch + H2O |
- |
Lactococcus lactis |
maltose + maltotriose |
- |
? |
3.2.1.41 | starch + H2O |
- |
Lactococcus lactis IBB500 |
maltose + maltotriose |
- |
? |
3.2.1.41 | starch + H2O |
the enzyme can degrade both the alpha-1,4 and alpha-1,6-linkages of alpha-glucans |
Sulfolobus acidocaldarius |
D-glucose + maltose + maltotriose |
- |
? |
3.2.1.41 | starch + H2O |
the enzyme can degrade both the alpha-1,4 and alpha-1,6-linkages of alpha-glucans |
Sulfolobus acidocaldarius DSM 639 |
D-glucose + maltose + maltotriose |
- |
? |
3.2.1.41 | starch + H2O |
- |
Pyrobaculum calidifontis |
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose + D-glucose |
- |
? |
3.2.1.41 | starch + H2O |
- |
Pyrobaculum calidifontis VA1 |
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose + D-glucose |
- |
? |
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 | 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 |
- |
? |