| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | in the crumb of fresh white wheat bread, starch is fully gelatinized. Its molecular and three-dimensional structure are major factors limiting the rate of its digestion. In situ modification of starch during bread making with starch-modifying enzymes (maltogenic amylase and amylomaltase) and analysis of the impact thereof on bread characteristics, starch retrogradation and digestibility, overview. Maltogenic amylase treatment increases the relative content of short amylopectin chains. This results in lower starch retrogradation and crumb firmness upon storage, and reduces extent (up to 18%) of in vitro starch digestion for fresh and stored breads. Amylomaltase only modestly shortens amylose chains and has no measurable impact on amylopectin structure. Modification with this enzyme leads to slower bread crumb firming but does not influence starch digestibility | Thermus thermophilus |
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus thermophilus | O87172 | - |
- |
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| commercial preparation | - |
Thermus thermophilus | - |
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | in the crumb of fresh white wheat bread, starch is fully gelatinized. Its molecular and three-dimensional structure are major factors limiting the rate of its digestion. In situ modification of starch during bread making with starch-modifying enzymes (maltogenic amylase and amylomaltase) and analysis of the impact thereof on bread characteristics, starch retrogradation and digestibility, overview. Maltogenic amylase treatment increases the relative content of short amylopectin chains. This results in lower starch retrogradation and crumb firmness upon storage, and reduces extent (up to 18%) of in vitro starch digestion for fresh and stored breads. Amylomaltase only modestly shortens amylose chains and has no measurable impact on amylopectin structure. Modification with this enzyme leads to slower bread crumb firming but does not influence starch digestibility, detailed overview. In vitro analysis of starch digestion in freeze-dried bread crumb | Thermus thermophilus | ? | - |
- |
| Synonyms | Comment | Organism |
|---|---|---|
| AMM | - |
Thermus thermophilus |
| amylomaltase | - |
Thermus thermophilus |
| MalQ | - |
Thermus thermophilus |
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35 | - |
assay at | Thermus thermophilus |
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
assay at | Thermus thermophilus |
| General Information | Comment | Organism |
|---|---|---|
| physiological function | enzyme amylomaltase (AMM) from Thermus thermophilus is a thermo-active 4-alpha-glucanotransferase. It catalyzes the transfer of linear glucan segments from the donor amylose (AM) to the acceptor non-reducing end of the amylopectin (AP) chains via a disproportionation reaction. In a model starch system, AMM can in situ change starch fine molecular structure by elongating the AP chains at the expense of the length of AM chains resulting in significantly lower extent and rate of starch digestion | Thermus thermophilus |