Wheat flour replacement from 22.5% up to 45% by incorporation of ternary blends of teff (T), 25 green pea (GP) and buckwheat (BW) flours provided technologically viable and acceptable sensory rated 26 multigrain breads with superior nutritional value compared to the 100% wheat flour (WT) counterparts. 27Blended breads exhibited superior nutritional composition, larger amounts of bioaccessible polyphenols, 28 higher anti-radical activity, and lower and slower starch digestibility. Simultaneous lower rapidly digestible 29 starch (57.1%) and higher slowly digestible starch (12.9%) and resistant starch (2.8%) contents (g per 100 g 30 fresh bread), considered suitable nutritional trends for dietary starch fractions, were met by the blend 31 formulated 7.5% T, 15% GP, 15% BK. The associated mixture that replaced 37.5% WT, showed a rather 32 lower extent and slower rate of starch hydrolysis with medium-low values for C∞, and H90, and lowest k, and 33 intermediate expected Glycaemic Index (86). All multigrain breads can be labelled as source of dietary fibre 34 (≥3 g dietary fibre/100 g bread). A slow release and absorption of glucose may be generated in a food matrix according to the 56 processing conditions and surrounding ingredients (Lehmann & Robin, 2007), encompassing beneficial 57 effects in the management of diabetes and hyperlipidemia (Jenkins, 2007). Native cereal starches are ideal 58 sources of slowly digestible starch (SDS) (>50%), and the slow progressive digestion property is realized by 59 a layer-by-layer inside-outside (radial) digestion process (Zhang, Ao, & Hamaker., 2006a). Mechanical and 60 thermal treatments change the structure and digestibility of starch. Thermal treatments such as the cooking 61 process completely destroys the semicrystalline structure of native starch granules and causes the loss of 62 SDS and resistant starch (RS) and increases rapid digestible starch (RDS) (Zhang, Venkatachalam, & 63 Hamaker, 2006b). In cereal products, the starch gelatinisation extent, which is mainly controlled by the 64 moisture level and the cooking time and temperature influences the formation of SDS (Englyst, Vinory, 65 Englyst, & Lang, 2003). In bread dough, although formation of resistant starch (RS3) may occur in the high 66 water-containing parts during cooling, a large portion of starch is gelatinised during cooking and induces a 67 rapid digestibility of starch (Bravo, Englyst, & Hudson, 1998). In extruded cooked cereal products such as 68 breakfast cereals, in addition to the thermal treatment, the high pressure and shear forces destroy the 69 starch granular structure and increase its gelatinisation extent, making it more available to amylolytic 70 enzymes (Le François, 1989). On the contrary, in pasta, a dense protein network is formed, which limits the 71 accessibility of α-amylase to the starch and restricts the diffusion of water molecules to the starch granules. 72 4 As a consequence, a reduction of the extent of starch gelatinisation takes place (Englyst et al., 1992). 73Fu...

Nine commercial enzyme preparations and two laboratory-designed mixes with amylase and/or pentosanase/xylanase activity were used to prepare bread samples, and the effects on bread quality and keeping properties were determined. With the doses added, enzymes significantly shortened fermentation time without affecting the pH or the machinability of the doughs. Bread with an improved volume, a greater intensity of aroma and a softer texture was obtained. Loaves had a less intense and characteristic taste and, in some cases, an uneven grain. All enzymes delayed bread firming, but rates varied with each preparation. Factor analysis classified bread samples according to their composition and source.

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BackgroundMany proteins with tandem repeats in their sequence have been described and classified according to the length of the repeats: I) Repeats of short oligopeptides (from 2 to 20 amino acids), including structural cell wall proteins and arabinogalactan proteins. II) Repeats that range in length from 20 to 40 residues, including proteins with a well-established three-dimensional structure often involved in mediating protein-protein interactions. (III) Longer repeats in the order of 100 amino acids that constitute structurally and functionally independent units. Here we analyse ShooT specific (ST) proteins, a family of proteins with tandem repeats of unknown function that were first found in Leguminosae, and their possible similarities to other proteins with tandem repeats.ResultsST protein sequences were only found in dicotyledonous plants, limited to several plant families, mainly the Fabaceae and the Asteraceae. ST mRNAs accumulate mainly in the roots and under biotic interactions. Most ST proteins have one or several Domain(s) of Unknown Function 2775 (DUF2775). All deduced ST proteins have a signal peptide, indicating that these proteins enter the secretory pathway, and the mature proteins have tandem repeat oligopeptides that share a hexapeptide (E/D)FEPRP followed by 4 partially conserved amino acids, which could determine a putative N-glycosylation signal, and a fully conserved tyrosine. In a phylogenetic tree, the sequences clade according to taxonomic group. A possible involvement in symbiosis and abiotic stress as well as in plant cell elongation is suggested, although different STs could play different roles in plant development.ConclusionsWe describe a new family of proteins called ST whose presence is limited to the plant kingdom, specifically to a few families of dicotyledonous plants. They present 20 to 40 amino acid tandem repeat sequences with different characteristics (signal peptide, DUF2775 domain, conservative repeat regions) from the described group of 20 to 40 amino acid tandem repeat proteins and also from known cell wall proteins with repeat sequences. Several putative roles in plant physiology can be inferred from the characteristics found.

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Kunitz proteinase inhibitors in legumes have mainly been described as defence and storage proteins. Here, we report a Kunitz trypsin inhibitor, encoded by the CaTPI-1 gene from Cicer arietinum. The transcription of this gene mainly occurs in seedling vegetative organs, and is affected by the light and growth stages. The recombinant TPI-1 protein expressed in E. coli was seen to be an efficient inhibitor of trypsin. After the generation of polyclonal antibodies against recombinant TPI-1 protein, the protein was located in the cell wall of elongating epicotyls and radicles by Western-blot experiments, in agreement with the transcription pattern. These results, together with the fact that both CaTPI-1 mRNA and protein levels decreased with epicotyl growth, suggest a possible role in the elongation of seedling epicotyls and radicles. Immunolocalization analyses of the TPI-1 protein indicated that it is abundant in the cell walls of both immature primary xylem cells and surrounding parenchyma cells. This location has led us to explore potential functions for TPI-1 protein in vascular tissue during seedling elongation.