The role of the gluten network in the crispness of bread crust

Crispness features of baked products strongly determine consumer acceptability. For many baked products, such as bread, the outer crust gives the crispy sensation. Confocal scanning laser microscopy of the structure of bread crust revealed a continuous protein phase and a discontinuous non-gelatinized starch phase in the outer crust. In contrast, the crumb and inner crust, showed a gelatinized starch network associated with a protein network. The role of the protein phase of the outer crust in determining crispness has been studied. During storage, the crispness of bread crust alters as a result of changes in water content/activity resulting from moisture redistribution within the bread and between the bread and its environment. Water content was affected by the flour protein content and by selectively modifying the crust protein phase of a model bread with enzymes, as well as by storing breads at high and low relative humidity (80-40% RH). Protease modification resulted in a lower water content and activity in the crust during the first hours of storage. In contrast, modification by transglutaminase had the opposite effect and gave rise to higher water retention of the crust compared to the un-treated d bread. This shows that modification of the protein network can be used to regulate the water holding capacity of the crust. Sensory analysis confirmed the retention of crispness in protease modified bread crust after 2 h storage at 80% RH conditions, whereas both the untreated and transglutaminase-treated breads lost their crispness. A negative relationship between water activity/content and crispness was found. Modification of the starch phase of the crust by alpha-amylase produced a bread crust with a low water activity. However, a steep increase in the water activity was observed after 2 h storage at 80% RH with a concomitant loss of crispness. These results indicate an important role of the gluten network in determining crust properties. (c) 2006 Elsevier Ltd. All rights reserved.