Koen J.A. Jansens

Impact of acid and alkaline pretreatments on the molecular network of wheat gluten and on the mechanical properties of compression-molded glassy wheat gluten bioplastics.

Wheat gluten can be converted into rigid biobased materials by high-temperature compression molding at low moisture contents. During molding, a cross-linked protein network is formed. This study investigated the effect of mixing gluten with acid/alkali in 70% ethanol at ambient temperature for 16 h followed by ethanol removal, freeze-drying, and compression molding at 130 and 150 °C on network formation and on types of cross-links formed. Alkaline pretreatment (0-100 mmol/L sodium hydroxide or 25 mmol/L potassium hydroxide) strongly affected gluten cross-linking, whereas acid pretreatment (0-25 mmol/L sulfuric acid or 25 mmol/L hydrochloric acid) had limited effect on the gluten network. Molded alkaline-treated gluten showed enhanced cross-linking but also degradation when treated with high alkali concentrations, whereas acid treatment reduced gluten cross-linking. β-Elimination of cystine and lanthionine formation occurred more pronouncedly at higher alkali concentrations. In contrast, formation of disulfide and nondisulfide cross-links during molding was hindered in acid-pretreated gluten. Bioplastic strength was higher for alkali than for acid-pretreated samples, whereas the flexural modulus was only slightly affected by either alkaline or acid pretreatment. Apparently, the ratio of disulfide to nondisulfide cross-links did not affect the mechanical properties of rigid gluten materials.

Proteins of Amaranth (Amaranthus spp.), Buckwheat (Fagopyrum spp.), and Quinoa (Chenopodium spp.): A Food Science and Technology Perspective

There is currently much interest in the use of pseudocereals for developing nutritious food products. Amaranth, buckwheat, and quinoa are the 3 major pseudocereals in terms of world production. They contain high levels of starch, proteins, dietary fiber, minerals, vitamins, and other bioactives. Their proteins have well-balanced amino acid compositions, are more sustainable than those from animal sources, and can be consumed by patients suffering from celiac disease. While pseudocereal proteins mainly consist of albumins and globulins, the predominant cereal proteins are prolamins and glutelins. We here discuss the structural properties, denaturation and aggregation behaviors, and solubility, as well as the foaming, emulsifying, and gelling properties of amaranth, buckwheat, and quinoa proteins. In addition, the technological impact of incorporating amaranth, buckwheat, and quinoa in bread, pasta, noodles, and cookies and strategies to affect the functionality of pseudocereal flour proteins are discussed. Literature concerning pseudocereal proteins is often inconsistent and contradictory, particularly in the methods used to obtain globulins and glutelins. Also, most studies on protein denaturation and techno-functional properties have focused on isolates obtained by alkaline extraction and subsequent isoelectric precipitation at acidic pH, even if the outcome of such studies is not necessarily relevant for understanding the role of the native proteins in food processing. Finally, even though establishing in-depth structure-function relationships seems challenging, it would undoubtedly be of major help in the design of tailor-made pseudocereal foods.

Importance of Thiol-Functionalized Molecules for the Structure and Properties of Compression-Molded Glassy Wheat Gluten Bioplastics

High-temperature compression molding of wheat gluten at low water levels yields a rigid plastic-like material. We performed a systematic study to determine the effect of additives with multiple thiol (SH) groups on gluten network formation during processing and investigate the impact of the resulting gluten network on the mechanical properties of the glassy end product. To this end, a fraction of the hydroxyl groups of different polyols was converted into SH functionalities by esterifying with 3-mercaptopropionic acid (MPA). The monofunctional additive MPA was evaluated as well. During low-temperature mixing SH-containing additives decreased the gluten molecular weight, whereas protein cross-linking occurred during high-temperature compression molding. The extent of both processes depended on the molecular architecture of the additives and their concentration. After molding, the material strength and failure strain increased without affecting the modulus, provided the additive concentration was low. The strength decreased again at too high concentrations for polyols with low SH functionalization. Attributing these effects solely to the interplay of plasticization and the SH-facilitated introduction of cross-links is inadequate, since an improvement in both strength and failure strain was also observed in the presence of high levels of MPA. It is hypothesized that, regardless of the molecular structure of the additive, the presence of SH-containing groups induces conformational changes which contribute to the mechanical properties of glassy gluten materials.

Ultrasonic Characterization of Amyloid-Like Ovalbumin Aggregation

Thermal processing conditions, pH, and salt content affect the formation of egg white ovalbumin amyloid, which was investigated using high-precision measurements of ultrasonic velocity and attenuation. These were related to fluorescence and particle size measurements. Fluorescence changes indicated the formation of amyloid-like aggregates that was enhanced by increasing time–temperature treatments. The ultrasonic velocity of ovalbumin after heating at neutral pH (60 min at 70 or 80 °C) was lower than that of unheated ovalbumin, whereas the attenuation was higher. The decrease in the velocity represents increased compressibility associated with a change in the compactness of the protein, whereas changes in attenuation are due to protein conformational changes. Heating ramp studies revealed transitions at approximately 58 and 73 °C. During heating at a constant temperature, the ultrasonic velocity decreased slowly with increasing heating time, indicating an increase in ovalbumin compressibility. It is suggested that the obtained amyloid-like ovalbumin aggregates contain a compact core surrounded by loosely packed protein segments.