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- 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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| 2. |
- 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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| 3. |
- 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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