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| 2. |
- Armoniené, Rita, et al.
(författare)
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Impact of Combined Drought and Heat Stress and Nitrogen on Winter Wheat Productivity and End-Use Quality
- 2022
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Ingår i: Agronomy. - : MDPI AG. - 2073-4395. ; 12
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Tidskriftsartikel (refereegranskat)abstract
- Water deficit and heat stress are the main abiotic stresses affecting the yield and quality of winter wheat. The increasing frequency of the simultaneous occurrence of these two stresses might threaten global food security and drives the need to breed resilient high-quality cultivars. The aim of this study was to evaluate the grain yield, quality and gluten protein characteristics in 50 winter wheat cultivars and breeding lines during the harvest years of 2018 and 2019. The yield and grain quality components were affected more severely by the combined heat and drought in 2019 than the drought in 2018. Two nitrogen (N) fertilization regimes were studied, sustainable (S, 15/100/30 kg N ha(-1)) and high-input (HI, 15/100/100 kg N ha(-1)). The yield was higher in HI trials compared to S trials by 2.2 t ha(-1) in 2018 and by 2.4 t ha(-1) in 2019. Higher protein content and sedimentation volume and lower yield, test weight and starch content were observed under combined heat and drought stress in 2019 compared to 2018. Genotypes containing the Glu-D1 x5-y10 allele exhibited the higher amounts of unextractable polymeric proteins (%UPP = 58.5%) in gluten studied by size exclusion liquid chromatography (SE-HPLC) as compared to Glu-D1 x2-y12 allele (%UPP = 54.3%). Genotype was the main determinant of gluten protein characteristics regardless of the nitrogen application and the abiotic stress conditions. The results suggest that the relatively mild drought and heat events in Lithuania might not threaten gluten quality in the future; however, breeding efforts should be directed towards improved drought and heat stress resistance to ensure stable wheat productivity in the region.
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| 3. |
- Berger Ceresino, Elaine, et al.
(författare)
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Morphological and structural heterogeneity of solid gliadin food foams modified with transglutaminase and food grade dispersants.
- 2020
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Ingår i: Food Hydrocolloids. - : Elsevier BV. - 0268-005X .- 1873-7137. ; 108
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Tidskriftsartikel (refereegranskat)abstract
- We show in this study the impact of transglutaminase (SB6), glycerol (Gly) and linoleic acid (LA) on the development of gliadin (Glia) solid edible foams. Two concentrations of SB6 were tested, 0.58 U/g and 1.17 U/g, and sufficiently high concentration of SB6 was found essential to crosslink the gliadins. Greater cross-linking in foam prepared with gliadin and 1.17 U/g of SB6 (2-TG-Glia) was followed by an increase of the size of the bubbles as well as improved bubble spatial homogeneity when compared to the non-treated gliadin foam (0-Glia). The inclusion of Gly had little effect on the periodic morphology of 2-TG-Glia, and the formed bubbles decreased in size. The 3D images of 2-TG-Glia revealed that the boundaries of the foams were less defined as observed by x-ray tomography. Nanomorphology studied by SAXS indicated that Gly impared the unfolding ofgliadin in the foam. The addition of linoleic acid (LA) in the foams caused formation of the discontinous Glia network with large and spaced bubbles as revealed by x-ray tomograms. The synergistic interactions of Glia and LA led to the formation of lamellar phases in the foams as observed by SAXS. The results from this study show gliadin as a promising resource to create diverse new aerated foods and contribute to achieve the demand for plant proteins with great foaming functionality. The addition of food-grade dispersants such as, glycerol andlinoleic acid, show a versatility and suitability of gliadin for new food applications such as breakfast cereals and snacks.
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| 4. |
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| 5. |
- Blomfeldt, Thomas O. J., et al.
(författare)
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Mechanical Properties and Network Structure of Wheat Gluten Foams
- 2011
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Ingår i: Biomacromolecules. - : American Chemical Society (ACS). - 1525-7797 .- 1526-4602. ; 12:5, s. 1707-1715
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Tidskriftsartikel (refereegranskat)abstract
- This Article reports the influence of the protein network structure on the mechanical properties of foams produced from commercial wheat gluten using freeze-drying. Foams were produced from alkaline aqueous solutions at various gluten concentrations with or without glycerol, modified with bacterial cellulose nanosized fibers, or both. The results showed that 20 wt % glycerol was sufficient for plasticization, yielding foams with low modulus and high strain recovery. It was found that when fibers were mixed into the foams, a small but insignificant increase in elastic modulus was achieved, and the foam structure became more homogeneous. SEM indicated that the compatibility between the fibers and the matrix was good, with fibers acting as bridges in the cell walls. IR spectroscopy and SE-HPLC revealed a relatively low degree of aggregation, which was highest in the presence of glycerol. Confocal laser scanning microscopy revealed distinct differences in HMW-glutenin subunits and gliadin distributions for all of the different samples.
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| 6. |
- Blomfeldt, Thomas O. J., et al.
(författare)
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Novel freeze-dried foams from glutenin- and gliadin-rich fractions
- 2012
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Ingår i: RSC Advances. - : Royal Society of Chemistry (RSC). - 2046-2069. ; 2:16, s. 6617-6627
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Tidskriftsartikel (refereegranskat)abstract
- This is the first study on freeze-dried foams prepared from glutenin- and gliadin-rich fractions of wheat gluten and blends thereof. It was found that the foam density and stiffness could be controlled by a suitable choice of the glutenin/gliadin ratio. The glutenin-rich samples had the highest foam densities and the density decreased with increasing gliadin content. The compression modulus also decreased with increasing gliadin content, which was explained by the decrease in foam density, a more open porosity and the more aggregated/polymerized structure in the presence of glutenin. IR and SE-HPLC revealed that the least aggregated foams were those consisting only of the gliadin-rich fraction. Confocal laser scanning microscopy revealed the presence of both HMW-glutenin and gliadin (to a certain extent probably resisting the ethanol extraction process) in the glutenin-rich foams. SAXS indicated that the gliadin-rich fraction contributed with weakly correlated protein aggregates with a characteristic distance of 40-43 Å.
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| 7. |
- Ceresino, E. B., et al.
(författare)
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Impact of gluten separation process and transglutaminase source on gluten based dough properties
- 2019
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Ingår i: Food Hydrocolloids. - : Elsevier. - 0268-005X .- 1873-7137. ; 87, s. 661-669
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Tidskriftsartikel (refereegranskat)abstract
- This study evaluated the effect of the wheat gluten (WG) separation process and transglutaminase (TG) microbial source on WG dough quality, and opportunities to use these factors to tailor dough quality. Two types of gluten (harshly and mildly separated), two types of TG (commercial and novel SB6), and three TG concentrations were evaluated for effects on dough mixing properties, protein structure and solubility. Mildly separated gluten improved dough development parameters, resulting into higher values of most compared with harshly separated gluten. Despite more strongly cross-linked proteins being found in the harshly separated gluten, both gluten types showed similar levels of cross-linking at optimum mixing time, although differences in the secondary protein structure were indicated. Thus, disulfide-sulfhydryl exchange reactions were found to be promoted by mixing, although restrictions on establishment of new bonds because of prior cross-links in the material were clearly indicated. Degree of polymerization in doughs made from mildly separated gluten increased to varying extents with TG addition depending on TG source and concentration. Thus, for the first time, we show that an appropriate combination of WG separation procedure and TG source can be used to tailor gluten dough end-use properties.
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| 8. |
- Ceresino, Elaine Berger, et al.
(författare)
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Lupin Protein Isolate Structure Diversity in Frozen-Cast Foams : Effects of Transglutaminases and Edible Fats
- 2021
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Ingår i: Molecules (Basel, Switzerland). - : MDPI AG. - 1420-3049. ; 26:6
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Tidskriftsartikel (refereegranskat)abstract
- This study addresses an innovative approach to generate aerated foods with appealing texture through the utilization of lupin protein isolate (LPI) in combination with edible fats. We show the impact of transglutaminases (TGs; SB6 and commercial), glycerol (Gly), soy lecithin (Lec) and linoleic acid (LA) on the micro- and nanostructure of health promoting solid foods created from LPI and fats blends. 3-D tomographic images of LPI with TG revealed that SB6 contributed to an exceptional bubble spatial organization. The inclusion of Gly and Lec decreased protein polymerization and also induced the formation of a porous layered material. LA promoted protein polymerization and formation of homogeneous thick layers in the LPI matrix. Thus, the LPI is a promising protein resource which when in blend with additives is able to create diverse food structures. Much focus has been placed on the great foamability of LPI and here we show the resulting microstructure of LPI foams, and how these were improved with addition of TGs. New food applications for LPI can arise with the addition of food grade dispersant Lec and essential fatty-acid LA, by improved puffiness, and their contributing as replacer of chemical leavening additives in gluten-free products.
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| 9. |
- Ceresino, Elaine Berger, et al.
(författare)
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Processing conditions and transglutaminase sources to "drive" the wheat gluten dough quality
- 2020
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Ingår i: Innovative Food Science & Emerging Technologies. - : Elsevier BV. - 1466-8564 .- 1878-5522. ; 65
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Tidskriftsartikel (refereegranskat)abstract
- Gluten proteins are highly impacting the quality of various gluten-based products, and transglutaminases (TGs) are used to influence the protein cross-linking. In this study we monitored the interplay of "harsh" and "mild" gluten processing for dough mixing and pasta-like sheet production and TGs from a commercial and newly sourced bacteria (SB6). Despite the harshly separated gluten presenting strongly cross-linked proteins in the beginning of the mixing, similar levels of polymerization were achieved at the optimum mixing time but with differences in the secondary protein structure. TG addition increased polymerization in wheat doughs, possibly as a result of increased glutenin polymerization, while gliadins become more soluble with SB6. This enzyme also dramatically increased polymerization in mild gluten. These results show that an adequate investigation when using TGs and gluten from various origins is necessary to adequately predict the quality in various gluten-based products, thus, of great relevance to the food industry. Industrial relevance: Currently, there is a mounting trend towards the modification of gluten proteins to improve technological features and functionality. In breadmaking, when weak Hour (low protein content) is used or general stabilization is desired for technological purposes, additives can be used to stabilize the gluten protein matrix. The use of transglutaminase (TG) has grown in popularity as they promote specific cross-linking between residues of glutamine and lysine in proteins. Another way of improving dough functionality is by increasing the oxidation of disulfide groups by adding gluten which is a co-product of the starch industry. Industrial production of gluten includes the use of heating and shear forces, which may impact gluten dough-forming ability. Thus, increased understanding of the interplay of gluten processing and the impact of choice of the TG origin in gluten dough quality is highly applicable in food industry.
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| 10. |
- Ceresino, Elaine B., et al.
(författare)
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Transglutaminase from newly isolated Streptomyces sp CBMAI 1617 : Production optimization, characterization and evaluation in wheat protein and dough systems
- 2018
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Ingår i: Food Chemistry. - : ELSEVIER SCI LTD. - 0308-8146 .- 1873-7072. ; 241, s. 403-410
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Tidskriftsartikel (refereegranskat)abstract
- The popularity of transglutaminase (TG) by the food industry and the variation in functionality of this enzyme from different origins, prompted us to isolate and evaluate a high-yielding TG strain. Through the statistical approaches, Plackett-Burman and response surface methodology, a low cost fermentation media was obtained to produce 6.074 +/- 0.019 U mL(-1) of TG from a novel source; Streptomyces sp. CBMAI 1617 (SB6). Its potential exploitation was compared to commonly used TG, from Streptomyces mobaraensis. Biochemical and FT-IR studies indicated differences between SB6 and commercial TG (Biobond (TM) TG-M). Additions of TG to wheat protein and flour based doughs revealed that the dough stretching depended on the wheat protein fraction, TG amount and its origin. A higher degree of cross-linking of glutenins and of inclusion of gliadin in the polymers was seen for SB6 as compared to commercial TG. Thus, our results support the potential of SB6 to tailor wheat protein properties within various food applications.
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