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Besides an appealing texture and taste, gluten-free products should feature a well-balanced nutrient profile, since celiac disease or chronic inflammations are likely to induce malnutrition for involved patients. Due to their composition, pseudocereals represent a promising ingredient to improve nutrient profile of gluten-free bread. The objective of this study was to investigate the impact of quinoa bran on gluten-free bread quality, focusing on volume, pore size and sensory acceptance. The impact of quinoa bran was studied in a gluten-free bread formulation. Five different quinoa bran and two whole grain flour concentrations were evaluated and compared to a control formulation based on rice and corn flour. The rheological properties of quinoa bran as well as the effect on dough development up to a replacement level of 80 % were investigated. Baking tests were carried out, and loaf volume, crumb firmness and sensory characteristics were determined. Quinoa fractions significantly increased carbon dioxide formation (p

Patients suffering from coeliac disease have to avoid traditional cereals-based products and depend on the availability of gluten-free alternatives. The gluten-free bread matrix and its foam stability are strongly affected by the choice of ingredients. In this study, the impact of quinoa white flour on bread quality parameters, in particular volume, has been investigated. The pseudocereal proved to be a suitable substrate for dough aeration using yeast, since considerably more glucose and a higher activity of α-glucosidase were found in comparison to rice and corn flour. Consequently, quinoa white flour was used to replace 40–100% of the rice and corn flour in a gluten-free control recipe. As a result, quinoa white flour enhanced the specific volume by 33%, which was related to the absence of bran components and the increased α-glucosidase activity. The significance of the latter was proven by separately adding sucrose and fungal amyloglucosidase to the control recipe. Moreover, the crumb featured homogeneous and finely distributed gas bubbles and the taste was not compromised. Thus, it was possible to improve the quality of gluten-free bread by using quinoa white flour, which might be a relief for coeliac patients.

DEAD box helicases catalyze the ATP-dependent destabilization of RNA duplexes. Whereas duplex separation is mediated by the helicase core shared by all members of the family, flanking domains often contribute to binding of the RNA substrate. The Thermus thermophilus DEAD-box helicase Hera (for "heat-resistant RNA-binding ATPase") contains a C-terminal RNA-binding domain (RBD). We have analyzed RNA binding to the Hera RBD by a combination of mutational analyses, nuclear magnetic resonance and X-ray crystallography, and identify residues on helix α1 and the C-terminus as the main determinants for high-affinity RNA binding. A crystal structure of the RBD in complex with a single-stranded RNA resolves the RNA-protein interactions in the RBD core region around helix α1. Differences in RNA binding to the Hera RBD and to the structurally similar RBD of the Bacillus subtilis DEAD box helicase YxiN illustrate the versatility of RNA recognition motifs as RNA-binding platforms. Comparison of chemical shift perturbation patterns elicited by different RNAs, and the effect of sequence changes in the RNA on binding and unwinding show that the RBD binds a single-stranded RNA region at the core and simultaneously contacts double-stranded RNA through its C-terminal tail. The helicase core then unwinds an adjacent RNA duplex. Overall, the mode of RNA binding by Hera is consistent with a possible function as a general RNA chaperone.

DEAD box helicases use the energy of ATP hydrolysis to remodel RNA structures or RNA/protein complexes. They share a common helicase core with conserved signature motifs, and additional domains may confer substrate specificity. Identification of a specific substrate is crucial towards understanding the physiological role of a helicase. RNA binding and ATPase stimulation are necessary, but not sufficient criteria for a bona fide helicase substrate. Here, we report single molecule FRET experiments that identify fragments of the 23S rRNA comprising hairpin 92 and RNase P RNA as substrates for the Thermus thermophilus DEAD box helicase Hera. Both substrates induce a switch to the closed conformation of the helicase core and stimulate the intrinsic ATPase activity of Hera. Binding of these RNAs is mediated by the Hera C-terminal domain, but does not require a previously proposed putative RNase P motif within this domain. ATP-dependent unwinding of a short helix adjacent to hairpin 92 in the ribosomal RNA suggests a specific role for Hera in ribosome assembly, analogously to the Escherichia coli and Bacillus subtilis helicases DbpA and YxiN. In addition, the specificity of Hera for RNase P RNA may be required for RNase P RNA folding or RNase P assembly.