EC Number   |
Application |
Reference |
|---|
   3.4.21.111 | biotechnology |
a maltose biding protein (MBP)-fused proaqualysin I expression plasmid is developed in which MBP is attached to the N-terminus of proaqualysin I. MBP appears effectively to suppress the folding-promoting activity of the N-terminal propeptide when the bacteria are grown at 30°C, leading to a massive accumulation of fusion aqualysin I precursor. The precursor is converted efficiently to mature aqualysin I by heat treatment at 70°C. By analyzing the product it is confirmed that aqualysin I is initially expressed as a whole fusion protein and then processed autocatalytically |
696814 |
| 3.4.21.111 | food industry |
presence of aqualysin 1 in bread dough has no impact on the specific bread volume and only limited impact on hardness, cohesiveness, springiness, resilience and chewiness, but impacts bread crumb coherence. Aualysin in dough is inhibited by wheat endogenous serine peptidase inhibitors during dough mixing and fermentation and starts hydrolyzing gluten proteins during baking above 80°C |
753630 |
| 3.4.21.111 | food industry |
the level of protein extractable in sodium dodecyl sulfate containing medium under non-reducing conditions from wheat dough decreases upon heating to a lesser extent when aqualysin is used than in control experiments. The higher level is caused by the release by Aq1 of peptides from the repetitive gluten protein domains during baking. The resultant thermoset gluten network in bread crumb is mainly made up by protein from non-repetitive gluten domains |
753633 |
| 3.4.21.111 | more |
C-terminal pro sequence of the enzyme functions as an intramolecular chaperone that stabilizes the partially unfolded structure of the protease domain, and thereby facilitates its secretion |
-, 673906 |
