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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

Verbauwhede, Annelien E., Lambrecht, Marlies A., Fierens, Ellen, Hermans, Senne, Shegay, Oksana, Brijs, Kristof, Delcour, Jan A.
Food chemistry 2018 v.264 pp. 118-125
Thermus aquaticus, baking, breadmaking, breads, chewiness, cohesion, dough, enzyme inhibitors, enzymes, fermentation, hardness, mixing, molecular weight, serine, sodium dodecyl sulfate, starch, temperature, texture, wheat, wheat gluten
The thermo-active serine peptidase aqualysin 1 (Aq1) of Thermus aquaticus was applied in bread making to study the relative contribution of thermoset gluten to bread crumb texture. Aq1 is active between 30 °C and 90 °C with an optimum activity temperature of around 65 °C. It is inhibited by wheat endogenous serine peptidase inhibitors during dough mixing and fermentation and starts hydrolyzing gluten proteins during baking above 80 °C when the enzyme is no longer inhibited and most of the starch is gelatinized and contributes to structure formation. Aq1 activity reduced the molecular weight of gluten proteins and significantly increased their extractability in sodium dodecyl sulfate containing medium. While it had no impact on the specific bread volume and only limited impact on hardness, cohesiveness, springiness, resilience and chewiness, it impacted bread crumb coherence. We conclude that starch has a greater impact on crumb texture than thermoset gluten.