Literature summary for 3.4.21.111 extracted from

Verbauwhede, A.E.; Lambrecht, M.A.; Fierens, E.; Hermans, S.; Shegay, O.; Brijs, K.; Delcour, J.A.
Thermo-reversible inhibition makes aqualysin 1 from Thermus aquaticus a potent tool for studying the contribution of the wheat gluten network to the crumb texture of fresh bread (2018), Food Chem., 264, 118-125 .

Search for more literature for 3.4.21.111

Application

Application	Comment	Organism
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	Thermus aquaticus

Inhibitors

Inhibitors	Comment	Organism	Structure
wheat fluor extract	presence of 0.6 microl wheat flour extract in the aqualysin (1.0 U) activity assay results in 37%, 36%, 32% or 28% lower activities when incubated at 30°C, 40°C, 50°C or 60°C, respectively	Thermus aquaticus

Organism

Organism	UniProt	Comment	Textmining
Thermus aquaticus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
commercial preparation	-	Thermus aquaticus	-

Synonyms

Synonyms	Comment	Organism
Aq1	-	Thermus aquaticus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
65	-	-	Thermus aquaticus

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
65	-	decrease in activity above	Thermus aquaticus

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Release 2023.1 (January 2023)