Bert Lagrain

The effects of different amylases on the rapid visco analysis rheological properties of starch were studied and the accompanying changes in the starch molecular properties were analyzed with high performance size exclusion chromatography. Different amylases affect the rheological properties of starch slurries and the molecular weight of the starch molecules to a degree depending on their mode of action and

Full baking of earlier partially baked (parbaked) bread can supply fresh bread to the consumer at any time of the day. When parbaked bread loaves were stored at -25, 4 or 23°C, the extent of crumb to crust moisture migration and amylopectin retrogradation differed with storage temperature, and the firming rate was evidently lowest during frozen storage. The extent of crumb to crust moisture migration during parbaked bread storage largely determined the mass of the fresh finished bread, and its crumb and crust moisture contents. Initial NMR proton mobility, initial resilience, the extent of amylopectin retrogradation and changes in firmness and resilience during storage of fully baked bread were affected by its crumb moisture content. The lowest firming rate was observed for finished bread resulting from parbaked bread stored at -25°C, while the highest firming rate was observed for finished bread from parbaked bread stored at 23°C.

ABSTRACT Bread crumb cellular structure and elasticity were monitored during aging and their relation to the main flour constituents, gluten and starch, was studied. The linear relation between the time-dependent slope of the linear part of the force-deformation curve, obtained in a static compressive test, and the shear modulus, obtained in quasi-static shear wave measurements, allowed calculating the Poisson’s ratio of bread crumb. This ratio and, thus, cell geometry remain unaffected during bread storage. While the elastic modulus of bread crumb strongly increased upon storage, image analysis and ultrasonic inspection, interpreted in the framework of the Biot-Allard model for porous structures, further confirmed that its cellular structure parameters did not change. Changing gluten properties in dough by means of redox agents had a profound impact on bread crumb density and its foam structure without affecting the rheological properties of the crumb cell walls. In agreement with the theory for cellular solids with open cells, bread with a lower density and a uniform crumb structure initially had a lower elastic modulus, which was maintained during aging, while bread with a higher density showed the opposite. Inclusion of an antifirming maltogenic exo-amylase in the recipe altered neither bread density, nor its macroscopic cellular structure parameters, but strongly affected the impact of storage on crumb texture. It was concluded that, without affecting starch properties or moisture content, the bread density, which is inter alia related to gluten properties, is a major determinant of bread crumb structure and texture during storage. In breads with a similar density and crumb foam structure, the evolution of crumb modulus during storage is determined by the changes in starch.

... It is therefore probable that the crosslinking of proteins through tyrosine residues does not significantly affect the formation of the gluten network or the structure of the gluten proteins compared with SS bonds ( [Hanft and Koehler, 2005] and [Pena et al., 2006] ). ...

... In contrast, during sugar-snap cookie dough making, high sugar and fat levels and low water levels lead to poor gluten hydration (Gaines, 1990), which results in non-elastic dough with minimal, if any, gluten development (Wade, 1988). ...

Solvent Retention Capacity (SRC) tests have originally been designed to predict flour functionality of North American wheat flours. A SRC profile consists of its Water Retention Capacity (WRC), Sodium Carbonate SRC (SCSRC), Sucrose SRC (SuSRC) and Lactic Acid SRC (LASRC) values. As the value of such tests when considering European wheat flours is rather unclear, we studied the chemical composition

To establish the relationship between biopolymer interactions, water dynamics, and crumb texture evolution in time, proton mobilities in starch and gluten model systems and bread were investigated with NMR relaxometry. Amylopectin recrystallization was observed as an increased amount of fast-relaxing protons, while network strengthening and changes in water levels were noted as a reduced mobility and amount, respectively, of slowly relaxing protons. Amylopectin recrystallization strengthened the starch network with concomitant inclusion of water and increased crumb firmness, especially at the beginning of storage. The inclusion of water and the thermodynamic immiscibility of starch and gluten resulted in local gluten dehydration during bread storage. Moisture migration from crumb to crust further reduced the level of plasticizing water of the biopolymer networks and contributed to crumb firmness at longer storage times. Finally, we noted a negative relationship between the mobility of slowly relaxing protons of crumb polymers and crumb firmness.

When Bacillus stearothermophilus α-amylase (BStA), Pseudomonas saccharophila α-amylase (PSA), or Bacillus subtilis α-amylase (BSuA) was added to a bread recipe to impact bread firming, amylose crystal formation was facilitated, leading to lower initial crumb resilience. Bread loaves that best retained their quality were those obtained when BStA was used. The enzyme hindered formation of an extended starch network, resulting in less water immobilization and smaller changes in crumb firmness and resilience. BSuA led to extensive degradation of the starch network during bread storage with release of immobilized water, eventually resulting in partial structure collapse and poor crumb resilience. The most important effect of PSA was an increased bread volume, resulting in smaller changes in crumb firmness and resilience. A negative linear relation was found between NMR proton mobilities of water and biopolymers in the crumb and crumb firmness. The slope of that relation gave an indication of the strength of the starch network.

The gluten proteins gliadin and glutenin are important for wheat flour functionality in bread making, where, during baking, they polymerize through a heat-induced sulfhydryl-disulfide exchange mechanism. A model system was used to study the kinetics of this reaction. Thus, gluten was subjected to hydrothermal treatment with the rapid visco analyzer (RVA) with holding temperatures of 80, 90, and 95 degrees C. At these temperatures, omega-gliadin solubility did not change, but the solubilities of alpha- and gamma-gliadin in 60% ethanol decreased according to first-order reaction kinetics. All reaction rate constants increased with temperature. The activation energies for the heat-induced exchange reaction were 110 and 147 kJ/mol for alpha- and gamma-gliadin, respectively. Starch did not influence the reaction rates of the association of alpha- and gamma-gliadin with glutenin. During gluten-starch model bread baking, glutenin oxidized first, and when the internal crumb temperature reached 100 degrees C, alpha- and gamma-gliadin cross-linked to glutenin, again following first-order reaction kinetics. The experimental findings and similarities in temperature conditions and reaction kinetics suggest that the RVA system can be instrumental in understanding gluten behavior in concentrated food systems, such as bread making.

Starch-water, gluten-water, and flour-water model systems as well as straight-dough bread were investigated with (1)H NMR relaxometry using free induction decay and Carr-Purcell-Meiboom-Gill pulse sequences. Depending on the degree of interaction between polymers and water, different proton populations could be distinguished. The starch protons in the starch-water model gain mobility owing to amylopectin crystal melting, granule swelling, and amylose leaching, whereas water protons lose mobility due to increased interaction with starch polymers. Heating of the gluten-water sample induces no pronounced changes in proton distributions. Heating changes the proton distributions of the flour-water and starch-water models in a similar way, implying that the changes are primarily attributable to starch gelatinization. Proton distributions of the heated flour-water model system and those of fresh bread crumb are very similar. This allows identifying the different proton populations in bread on the basis of the results from the model systems.

Two baking times (9 and 24 min) and storage temperatures (4 and 25 °C) were used to explore the impact of heat exposure during bread baking and subsequent storage on amylopectin retrogradation, water mobility, and bread crumb firming. Shorter baking resulted in less retrogradation, a less extended starch network and smaller changes in crumb firmness and elasticity. A lower storage temperature resulted in faster retrogradation, a more rigid starch network with more water inclusion and larger changes in crumb firmness and elasticity. Crumb to crust moisture migration was lower for breads baked shorter and stored at lower temperature, resulting in better plasticized biopolymer networks in crumb. Network stiffening, therefore, contributed less to crumb firmness. A negative relation was found between proton mobilities of water and biopolymers in the crumb gel network and crumb firmness. The slope of this linear function was indicative for the strength of the starch network.

... 4). During the final 20 min of bak-ing, only subtle changes in protein extractability were measured (Fig. ... Kristof Brijs and Bert La-grain wish to acknowledge the Industrial Research Fund (KU Leuven, Leuven, Belgium) and the Research Foundation Flanders (FWO, Brus-sels ...

The unique properties of the wheat grain reside primarily in the gluten-forming storage proteins of its endosperm. Wheat gluten's structural and functional properties have led to an expanding diversity of applications in food products. However, its viscoelastic properties and low water solubility also are very interesting features for nonfood applications. Moreover, gluten is annually renewable and perfectly biodegradable. In the processing and setting of gluten containing products, temperature plays a very important role. In this review, the structure and reactivity of gluten are discussed and the importance of sulfhydryl (SH) and disulfide (SS) groups is demonstrated. Wheat gluten aggregation upon thermosetting proceeds through direct covalent cross-linking in and between its protein groups, glutenin and gliadin. Predominant reactions include SH oxidation and SH/SS interchange reactions leading to the formation of SS cross-links. Additionally, thermal treatment of gluten can result in the formation of other than SS covalent bonds. We here review two main technological approaches to make gluten-based materials: wet processes resulting in thin films and dry processes, such as extrusion or compression molding, exploiting the thermoplastic properties of proteins under low moisture conditions and potentially resulting in very useful materials. Gluten bioplastics can also be reinforced with natural fibers, resulting in biocomposites. Although a lot of progress has been made the past decade, the current gluten materials are still outperformed by their synthetic polymer counterparts.