| 1. |
- Capezza, Antonio Jose, et al.
(författare)
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Carboxylated Wheat Gluten Proteins : A Green Solution for Production of Sustainable Superabsorbent Materials
- 2020
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Ingår i: Biomacromolecules. - : American Chemical Society (ACS). - 1525-7797 .- 1526-4602. ; 21:5, s. 1709-1719
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Tidskriftsartikel (refereegranskat)abstract
- Functionalized wheat gluten (WG) protein particles with the ability to absorb fluids within the superabsorbent range are presented. Ethyleneditetraacetic dianhydride (EDTAD), a nontoxic acylation agent, was used for the functionalization of the WG protein at higher protein content than previously reported and no additional chemical cross-linking. The 150-550 μm protein particles had 50-150 nm nanopores induced by drying. The EDTAD treated WG were able to absorb 22, 5, and 3 times of, respectively, water, saline and blood, per gram of dry material (g/g), corresponding to 1000, 150 and 100% higher values than for the as-received WG powder. The liquid retention capacity after centrifugation revealed that almost 50% of the saline liquid was retained within the protein network, which is similar to that for petroleum-based superabsorbent polymers (SAPs). An advantageous feature of these biobased particulate materials is that the maximum swelling is obtained within the first 10 min of exposure, that is, in contrast to many commercial SAP alternatives. The large swelling in a denaturation agent (6 M urea) solution (about 32 g/g) suggests that the secondary entangled/folded structure of the protein restricts protein network expansion and when disrupted allows the absorption of even higher amounts of liquid. The increased liquid uptake, utilization of inexpensive protein coproducts, easy scalable protocols, and absence of any toxic chemicals make these new WG-based SAP particles an interesting alternative to petroleum-based SAP in, for example, absorbent disposable hygiene products.
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| 2. |
- Capezza, Antonio Jose, et al.
(författare)
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Extrusion of Porous Protein-Based Polymers and Their Liquid Absorption Characteristics
- 2020
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Ingår i: Polymers. - : MDPI. - 2073-4360. ; 12:2
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Tidskriftsartikel (refereegranskat)abstract
- The production of porous wheat gluten (WG) absorbent materials by means of extrusion processing is presented for the future development of sustainable superabsorbent polymers (SAPs). Different temperatures, formulations, and WG compositions were used to determine a useful protocol that provides the best combination of porosity and water swelling properties. The most optimal formulation was based on 50 wt.% WG in water that was processed at 80 degrees C as a mixture, which provided a porous core structure with a denser outer shell. As a green foaming agent, food-grade sodium bicarbonate was added during the processing, which allowed the formation of a more open porous material. This extruded WG material was able to swell 280% in water and, due to the open-cell structure, 28% with non-polar limonene. The results are paving the way towards production of porous bio macromolecular structures with high polar/non-polar liquid uptake, using extrusion as a solvent free and energy efficient production technique without toxic reagents.
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| 3. |
- Capezza, Antonio Jose, et al.
(författare)
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High Capacity Functionalized Protein Superabsorbents from an Agricultural Co‐Product: A Cradle‐to‐Cradle Approach
- 2020
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Ingår i: Advanced Sustainable Systems. - : Wiley. - 2366-7486.
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Tidskriftsartikel (refereegranskat)abstract
- Synthesis of superabsorbent particles from nontoxic wheat gluten (WG) protein, as an industrial co‐product, is presented. A natural molecular cross‐linker named genipin (a hydrogenated glycoside) is used together with a dianhydride (ethylenediaminetetraacetic EDTAD), to enable the preparation of a material with a network structure capable of swelling up to ≈4000% in water and ≈600% in saline solution. This represents an increase in swelling by over 10 times compared to the already highly absorbing gluten reference material. The carboxylation (using EDTAD) and the cross‐linking of the protein result in a hydrogel with liquid retention capacity as high as 80% of the absorbed water remaining in the WG network on extensive centrifugation, which is higher than that of commercial fossil‐based superabsorbents. The results also show that more polar forms of the reacted genipin are more effectively grafted onto the protein, contributing to the swelling and liquid retention. Microscopy of the materials reveals extensive nanoporosity (300 nm), contributing to rapid capillarity‐driven absorption. The use of proteins from agricultural industries for the fabrication of sustainable protein superabsorbents is herein described as an emerging avenue for the development of the next generation daily‐care products with a minimal environmental impact.
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| 4. |
- Capezza, Antonio Jose
(författare)
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Sustainable Biobased Protein Superabsorbents from Agricultural Co-Products
- 2020
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Doktorsavhandling (övrigt vetenskapligt/konstnärligt)abstract
- The preparation of sustainable protein superabsorbents from agricultural industry side-streams is reported. Wheat gluten (WG), a co-product from the ethanol/starch industry, was processed into foams with sponge-like behavior and high liquid uptake. The materials were obtained by phase-separation of aqueous WG dispersions followed by ambient drying, or by lyophilization. The use of a natural and non-toxic cross-linker (genipin) resulted in foams with high water swelling properties (~18 g/g in 10 min). The rapid swelling may be of use in bio-based foams in e.g., sanitary pads.As an alternative, potato protein concentrate (PPC, side-stream from the starch industry), was functionalized and prepared as particles. The liquid swelling capacity was compared after acylation with five different agents. It is shown that the PPC can be acylated to replicate the chemistry of synthetic superabsorbent polymers (SAP), showing water swelling capacity >10 g/g. The acylation (using EDTAD) of WG suspensions resulted in protein particles with water and saline uptake of 22 and 5 g/g, respectively. Limited network stability was however observed when acylating WG in low-protein suspensions. This was addressed by mixing the acylated protein with genipin, which provided a stable protein network. The process gave functionalized particles with swelling capacity ~40 g/g and ~80 % retention of swelling in centrifuge retention tests.The extrusion of WG showed that porous WG with water uptake of 500 % can be produced. Further, the scalability of PPC production was pilot-tested by functionalizing potato fruit juice (PFJ), containing the potato protein in its soluble state before the industrial drying used to obtain PPC. This resulted in water swelling capacities >10 g/g, which was comparable to the PPC-functionalized materials. The results pave the way for future optimization of high-throughput production techniques using protein sources in mass production of sustainable protein-based SAPs.
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| 5. |
- 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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| 6. |
- Damian, Donath, et al.
(författare)
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Diversity of viruses in hard ticks (Ixodidae) from select areas of a wildlife-livestock interface ecosystem at Mikumi National Park, Tanzania
- 2020
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Ingår i: American Journal of BioScience. - : Science Publishing Group. - 2330-0159 .- 2330-0167. ; 8, s. 150-157
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Tidskriftsartikel (refereegranskat)abstract
- Many of the recent emerging infectious diseases have occurred due to the transmission of the viruses that have wildlife reservoirs. Arthropods, such as ticks, are known to be important vectors for spreading viruses and other pathogens from wildlife to domestic animals and humans. In the present study, we explored the diversity of viruses in hard ticks (Ixodidae) from select areas of a wildlife-livestock interface ecosystem at Mikumi National Park, Tanzania using a metagenomic approach. cDNA and DNA were amplified with random amplification and Illumina high-throughput sequencing was performed. The high-throughput sequenced data was imported to the CLC genomic workbench and trimmed based on quality (Q = 20) and length (≥ 50). The trimmed reads were assembled and annotated through Blastx using Diamond against the National Center for Biotechnology Information non-redundant database and its viral database. The MEGAN Community was used to analyze and to compare the taxonomy of the viral community. The obtained contigs and singletons were further subjected to alignment and mapping against reference sequences. The viral sequences identified were classified into bacteria, vertebrates, and invertebrates, plants, and protozoans viruses. Sequences related to known viral families; Retroviridae, Flaviviridae, Rhabdoviridae, Chuviridae, Orthomyxoviridae, Phenuiviridae, Totiviridae, Rhabdoviridae, Parvoviridae, Caulimoviridae, Mimiviridae and several Phages were reported. This result indicates that there are many viruses present in the study region, which we are not aware of and do not know the role they have or if they have the potential to spread to other species and cause diseases. Therefore, further studies are required to delineate the viral community present in the region over a large scale.
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| 7. |
- Das, Oisik, et al.
(författare)
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Naturally-occurring bromophenol to develop fire retardant gluten biopolymers
- 2020
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Ingår i: Journal of Cleaner Production. - : Elsevier. - 0959-6526 .- 1879-1786. ; 243
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Tidskriftsartikel (refereegranskat)abstract
- The aim of the study was to impart fire retardancy in wheat gluten polymer through naturally-occurring additives such as lanosol. The fire properties of lanosol were compared with two other conventional brominated fire retardants (Tetrabromobisphenol A and Hexabromocyclododecane). Samples containing fire retardants and gluten were prepared through compression moulding process and then characterised for their fire and mechanical properties. All fire retardants enhanced the reaction-to-fire and thermal properties of gluten while generating V-0 (i.e. vertical position and self-extinguished) ratings in the UL-94 test. The presence of all the fire retardants increased the modulus of the gluten polymer but the fire retardant particles were detrimental for the tensile strength. Nevertheless, lanosol addition delayed ignition and lowered peak heat release rate of gluten by the maximum amount, thereby leading to relatively higher fire performance index (compared to the other fire retardants). Lanosol also allowed the gluten to create a dense char barrier layer during burning that impeded the transfer of heat and flammable volatiles. The fact that only 4 wt% lanosol was able to cause self-extinguishment under direct flame and reduce peak heat release rate by a significant 50% coupled with its inherent occurrence in nature, raises the question if lanosol can be a potential fire retardant in polymeric systems, although it is a bromophenol.
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| 8. |
- Johansson Wensman, Jonas, et al.
(författare)
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Application of Viral Metagenomics for Study of Emerging and Reemerging Tick-Borne Viruses
- 2020
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Ingår i: Vector-Borne and Zoonotic Diseases. - : Mary Ann Liebert Inc. - 1530-3667 .- 1557-7759. ; 20, s. 557-565
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Tidskriftsartikel (refereegranskat)abstract
- Ticks are important vectors for different tick-borne viruses, some of which cause diseases and death in humans, livestock, and wild animals. Tick-borne encephalitis virus, Crimean-Congo hemorrhagic fever virus, Kyasanur forest disease virus, severe fever with thrombocytopenia syndrome virus, Heartland virus, African swine fever virus, Nairobi sheep disease virus, and Louping ill virus are just a few examples of important tick-borne viruses. The majority of tick-borne viruses have RNA genomes that routinely undergo rapid genetic modifications such as point mutations during their replication. These genomic changes can influence the spread of viruses to new habitats and hosts and lead to the emergence of novel viruses that can pose a threat to public health. Therefore, investigation of the viruses circulating in ticks is important to understand their diversity, host and vector range, and evolutionary history, as well as to predict new emerging pathogens. The choice of detection method is important, as most methods detect only those viruses that have been previously well described. On the other hand, viral metagenomics is a useful tool to simultaneously identify all the viruses present in a sample, including novel variants of already known viruses or completely new viruses. This review describes tick-borne viruses, their historical background of emergence, and their reemergence in nature, and the use of viral metagenomics for viral discovery and studies of viral evolution.
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| 9. |
- Markgren, Joel, et al.
(författare)
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Glutenin and Gliadin, a Piece in the Puzzle of their Structural Properties in the Cell Described through Monte Carlo Simulations
- 2020
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Ingår i: Biomolecules. - : MDPI. - 2218-273X. ; 10:8
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Tidskriftsartikel (refereegranskat)abstract
- Gluten protein crosslinking is a predetermined process where specific intra- and intermolecular disulfide bonds differ depending on the protein and cysteine motif. In this article, all-atom Monte Carlo simulations were used to understand the formation of disulfide bonds in gliadins and low molecular weight glutenin subunits (LMW-GS). The two intrinsically disordered proteins appeared to contain mostly turns and loops and showed "self-avoiding walk" behavior in water. Cysteine residues involved in intramolecular disulfide bonds were located next to hydrophobic peptide sections in the primary sequence. Hydrophobicity of neighboring peptide sections, synthesis chronology, and amino acid chain flexibility were identified as important factors in securing the specificity of intramolecular disulfide bonds formed directly after synthesis. The two LMW-GS cysteine residues that form intermolecular disulfide bonds were positioned next to peptide sections of lower hydrophobicity, and these cysteine residues are more exposed to the cytosolic conditions, which influence the crosslinking behavior. In addition, coarse-grained Monte Carlo simulations revealed that the protein folding is independent of ionic strength. The potential molecular behavior associated with disulfide bonds, as reported here, increases the biological understanding of seed storage protein function and provides opportunities to tailor their functional properties for different applications.
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| 10. |
- Rasheed, Faiza, et al.
(författare)
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Modeling to Understand Plant Protein Structure-Function Relationships-Implications for Seed Storage Proteins
- 2020
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Ingår i: Molecules. - : MDPI. - 1431-5157 .- 1420-3049. ; 25:4
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Forskningsöversikt (refereegranskat)abstract
- Proteins are among the most important molecules on Earth. Their structure and aggregation behavior are key to their functionality in living organisms and in protein-rich products. Innovations, such as increased computer size and power, together with novel simulation tools have improved our understanding of protein structure-function relationships. This review focuses on various proteins present in plants and modeling tools that can be applied to better understand protein structures and their relationship to functionality, with particular emphasis on plant storage proteins. Modeling of plant proteins is increasing, but less than 9% of deposits in the Research Collaboratory for Structural Bioinformatics Protein Data Bank come from plant proteins. Although, similar tools are applied as in other proteins, modeling of plant proteins is lagging behind and innovative methods are rarely used. Molecular dynamics and molecular docking are commonly used to evaluate differences in forms or mutants, and the impact on functionality. Modeling tools have also been used to describe the photosynthetic machinery and its electron transfer reactions. Storage proteins, especially in large and intrinsically disordered prolamins and glutelins, have been significantly less well-described using modeling. These proteins aggregate during processing and form large polymers that correlate with functionality. The resulting structure-function relationships are important for processed storage proteins, so modeling and simulation studies, using up-to-date models, algorithms, and computer tools are essential for obtaining a better understanding of these relationships.
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