Impact of aqualysin 1 peptidase from Thermus aquaticus on molecular scale changes in the wheat gluten network during bread baking.


KU Leuven, Laboratory of Food Chemistry and Biochemistry, Leuven Food Science and Nutrition Research Centre (LFoRCe), Kasteelpark Arenberg 20, B-3001 Leuven, Belgium. Electronic address: [Email]


The impact of Aqualysin 1 (Aq1), the thermo-active peptidase of Thermus aquaticus, on wheat albumin, globulin, gliadin and glutenin proteins during heat treatment of wheat dough and bread baking was examined. The level of protein extractable in sodium dodecyl sulfate containing medium under non-reducing conditions (SDS-EP-NR) from wheat dough decreases upon heating to a lesser extent when Aq1 is used than in control experiments. The higher SDS-EP-NR level is caused by the release by Aq1 of peptides from the repetitive gluten protein domains during baking. These peptides are also extractable from bread crumb with salt solution. The resultant thermoset gluten network in bread crumb is mainly made up by protein from non-repetitive gluten domains.


Amino acid analysis,Covalently heat-induced protein network,Heat-inactivated inhibition,Interconnected gluten peptides,Molecular weight distribution,Osborne type fractionation bread crumb,Sodium dodecyl sulfate extractability,