| 1. |
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| 2. |
- Blomfeldt, Thomas O. J., et al.
(author)
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Novel freeze-dried foams from glutenin- and gliadin-rich fractions
- 2012
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In: RSC Advances. - : Royal Society of Chemistry (RSC). - 2046-2069. ; 2:16, s. 6617-6627
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Journal article (peer-reviewed)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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| 3. |
- Das, Oisik, et al.
(author)
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The development of fire and microbe resistant sustainable gluten plastics
- 2019
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In: Journal of Cleaner Production. - : ELSEVIER SCI LTD. - 0959-6526 .- 1879-1786. ; 222, s. 163-173
-
Journal article (peer-reviewed)abstract
- This study shows the improvement of fire and microbe resistance of sustainable (protein) plastics (i.e. wheat gluten, WG), by using triethylene glycol diamine and dialdehyde. In addition, an anti-microbial agent (lanosol) was also used separately and in combination with the diamine/dialdehyde. The network formed by the diamine and dialdehyde, during the production of compression-moulded plates, resulted in high fire performance index, large amount of char and low thermal decomposition rate. The best fire resistance was obtained by the combination of the dialdehyde and lanosol, which also yielded a char with the intact surface. The peak-heat-release-rate of this material was only 38% of that of the pure gluten material. This material also showed anti-bacterial (E. coli) properties. However, the diamine was more effective than the combination of dialdehyde/lanosol. Gluten materials with diamine resisted mould growth during a 22 days test at a relative humidity of 100%. The gluten material with the lanosol applied to the sample surface resisted mould growth during a three-week test at both ambient temperature and 37 degrees C. Despite the relatively high contents of the difunctional reagents used (15 wt%), leading to an increased stiffness in most cases, only the network formed with glyoxal resulted in a decrease in water uptake as compared to the pure gluten material.
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| 4. |
- Diuk Andrade, Fabiana, et al.
(author)
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An insight into molecular motions and phase composition of gliadin/glutenin glycerol blends studied by 13C solid-state and 1H time-domain NMR
- 2018
-
In: Journal of Polymer Science, Part B: Polymer Physics. - : Wiley. - 0887-6266 .- 1099-0488. ; 56:9, s. 739-750
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Journal article (peer-reviewed)abstract
- Monitoring of the molecular motions and secondary structures of gliadin (Gli) and glutenin (Glu) in blends with 10, 20, 30, and 40% glycerol was performed by solid-state (SS) and time domain (TD) NMR spectroscopy. Increasing the glycerol content increased the relative amount of β-sheets and disordered structures, while decreasing α-helices in Gli/Glu–glycerol blends studied by 13C CPMAS NMR. For ≥20% glycerol samples, the protein side-chain mobility increased similarly for Gli and Glu. A higher proportion of α-helices versus β-sheets was found in Gli-glycerol blends compared with Glu–glycerol blends. Glycerol acted as “immobilized” in 10–20% glycerol Gli samples and was found mainly “free” in 30 and 40% glycerol Gli/Glu samples. During temperature experiments, 30 and 40% glycerol amounts impacted the dynamic molecular behavior of the Gli and Glu proteins differently than lipids, as observed by TD-NMR. The combination of TD-NMR together with SS-NMR showed details of the dynamic molecular variations in Gli/Glu protein structure and are promising techniques to monitor the molecular dynamics of plasticized proteins.
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| 5. |
- Johansson, Eva, et al.
(author)
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Wheat gluten polymer structures : The impact of genotype, environment, and processing on their functionality in various applications
- 2013
-
In: Cereal Chemistry. - 0009-0352 .- 1943-3638. ; 90:4, s. 367-376
-
Journal article (peer-reviewed)abstract
- For a number of applications, gluten protein polymer structures are of the highest importance in determining end-use properties. The present article focuses on gluten protein structures in the wheat grain, genotype- and environment-related changes, protein structures in various applications, and their impact on quality. Protein structures in mature wheat grain or flour are strongly related to end-use properties, although influenced by genetic and environment interactions. Nitrogen availability during wheat development and genetically determined plant development rhythm are the most important parameters determining the gluten protein polymer structure, although temperature during plant development interacts with the impact of the mentioned parameters. Glutenin subunits are the main proteins incorporated in the gluten protein polymer in extracted wheat flour. During dough mixing, gliadins are also incorporated through disulfide-sulfhydryl exchange reactions. Gluten protein polymer size and complexity in the mature grain and changes during dough formation are important for breadmaking quality. When using the gluten proteins to produce plastics, additional proteins are incorporated in the polymer through disulfide-sulfhydryl exchange, sulfhydryl oxidation, β-eliminations with lanthionine formation, and isopeptide formation. In promising materials, the protein polymer structure is changed toward β-sheet structures of both intermolecular and extended type and a hexagonal close-packed structure is found. Increased understanding of gluten protein polymer structures is extremely important to improve functionality and end-use quality of wheat- and gluten-based products.
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| 6. |
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| 7. |
- Kianersi, Farzad, et al.
(author)
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Biosynthesis of rutin changes in Capparis spinosa due to altered expression of its pathway genes under elicitors' supplementation
- 2020
-
In: Plant Cell Tissue and Organ Culture. - : Springer Nature. - 0167-6857 .- 1573-5044. ; 141:3, s. 619-631
-
Journal article (peer-reviewed)abstract
- Caper plant is (Capparis spinosa L.) a good source of rutin which plays a key role in the human diet. In this study, the effect of different concentrations of salicylic acid (SA) and methyl jasmonate (MeJA) on the weight of anther-derived calli and their rutin contents were assessed in caper plants. Also, we investigated the rutin content and expression pattern of some rutin related genes in leaves of caper plants at vegetative and fresh fruiting growth stages under SA and MeJA treatments. In the first experiment, the highest rutin contents were observed in anther-derived calli treated with 10 mu M MeJA and 100 mg L-1 SA after 2 weeks from initial treatments, which were 2.44 and 2.22-fold higher than control. Also, the treatment of caper plants with150 mu M MeJA and 100 mg L-1 SA resulted in a higher increase in the rutin content of leaves at the fresh fruiting stage (61.46 and 9.99 mg g(-1) DW, respectively), in the second experiment. Among the studied genes, the FLS gene showed the highest expression in the leaves of the MeJA- and SA-treated plants at vegetative growth stage, while in the fresh fruiting stage the highest expression was related to the RT gene. Use of 150 mu M MeJA and 100 mg L-1 SA enhanced the expression levels of the RT gene up to 7.36 and 2.89 times of the control, respectively. These results suggest that rutin content and the expression patterns of rutin biosynthesis genes in caper can be significantly enhanced by the SA and MeJA treatments in a growth stage-dependent manner. Key message Methyl jasmonate and salicylic acid treatments enhance the rutin contents of Capparis spinosa in vitro and in vivo and up-regulate the rutin biosynthetic related genes at two different growth stages.
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| 8. |
- Kianersi, Farzad, et al.
(author)
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Identification and tissue-specific expression of rutin biosynthetic pathway genes in Capparis spinosa elicited with salicylic acid and methyl jasmonate
- 2020
-
In: Scientific Reports. - : Springer Nature. - 2045-2322. ; 10:1
-
Journal article (peer-reviewed)abstract
- Capparis spinosa is an edible medicinal plant which is considered as an excellent source of rutin. Rutin is a glycoside of the flavonoid quercetin that has been reported to have a beneficial role in controlling various diseases such as hypertension, arteriosclerosis, diabetes, and obesity. In this study, the partial cDNA of four genes involved in the rutin biosynthetic pathway including 4-coumaroyl CoA ligase (4CL), flavonoid 3'-hydroxylase (F3'H), flavonol synthase (FLS) and flavonol-3-O-glucoside L-rhamnosyltransferase (RT) were identified in C.spinosa plants for the first time. The protein sequences of these genes shared high similarity with the same proteins in other plant species. Subsequently, the expression patterns of these genes as well as rutin accumulation in C.spinosa leaves treated with different concentrations of salicylic acid (SA) and methyl jasmonate (MeJA) and also in different tissues of Caper plants treated with 100 mgL(-1) SA and 150 mu M MeJA were evaluated. The expression of all four genes was clearly up-regulated and rutin contents increased in response to MeJA and SA treatments after 24 h. The highest rutin contents (5.30 mgg(-1) DW and 13.27 mgg(-1) DW), as well as the highest expression levels of all four genes, were obtained using 100 mgL(-1) SA and 150 mu M MeJA, respectively. Among the different tissues, the highest rutin content was observed in young leaves treated with 150 mu M MeJA, which corresponded to the expression of related genes, especially RT, as a key gene in the rutin biosynthetic pathway. These results suggest that rutin content in various tissues of C. spinosa can be enhanced to a significant extent by MeJA and SA treatments and the gene expression patterns of rutin-biosynthesis-related genes are regulated by these elicitors.
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| 9. |
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| 10. |
- Kuktaite, Ramune, et al.
(author)
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How the unuseful can be turned into sustainable and useful: novel potato protein bioplastics with unusual strength
- 2015
-
In: LTV-fakultetens faktablad.
-
Other publication (pop. science, debate, etc.)abstract
- In Southern Sweden the way potato starch is produced creates large amounts of by-product. This by-product consists of potato protein and non-edible com- pounds, which limits its use as food today. Improved uses of industrial by-product is of high interest for the future, and the- refore nding a better use of the potato proteins from potato starch production is needed.Through this collaboration pro- ject between the researchers at SLU Al- narp and Lyckeby Starch AB it has been shown that potato proteins are suitable for making potato protein bioplastics. Also, the bioplastics made from these potato proteins have shown unusual strenght and stretchiness, properties that could be suitable for a multi-layered packaging bag for potato chips.
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| 11. |
- Kuktaite, Ramune, et al.
(author)
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Monitoring Nanostructure Dynamics and Polymerization in Glycerol Plasticized Wheat Gliadin and Glutenin Films : Relation to Mechanical Properties
- 2016
-
In: ACS Sustainable Chemistry and Engineering. - : American Chemical Society (ACS). - 2168-0485. ; 4:6, s. 2998-3007
-
Journal article (peer-reviewed)abstract
- Gliadin and glutenin proteins with 10, 20, 30 and 40% of glycerol were compression molded into films (130 °C) and evaluated for protein polymerization, β-sheet structure and nano-structural morphology. Here, for the first time we show how different amounts of glycerol impact the nano-structure and functional properties of the gliadin and glutenin films. Most polymerized protein was found in the gliadin films with 20 and 30% glycerol, and in all the glutenin films (except 10%), by RP-HPLC. A β-sheet-rich protein structure was found to be high in the 10 and 20% glycerol gliadin films, and in the 20 and 30% glycerol glutenin films by FT-IR. Glycerol content of 20, 30 and 40% impacted the nano-structural morphology of the gliadin glycerol films observed by SAXS, and to a limited extent for 10 and 20% glycerol gliadin films revealed by WAXS. No ordered nano-structure was found for the glutenin glycerol films. The 20%, 30% and 40% glycerol films were the most tunable for specific mechanical properties. For the highest stiffness and strength, the 10% glycerol protein films were the best choice.
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| 12. |
- Mahmood, Rashid, et al.
(author)
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Assessment of antidiabetic potential and phytochemical profiling of Rhazya stricta root extracts
- 2020
-
In: BMC Complementary Medicine and Therapies. - : Springer Nature. - 2662-7671. ; 20:1
-
Journal article (peer-reviewed)abstract
- Background: Diabetes mellitus is a chronic disease characterized by hyperglycemia that may occur due to genetic, environmental or lifestyle factors. Natural remedies have been used to treat diabetes since long and many antidiabetic compounds of varied efficacies have been isolated from medicinal plants. Rhazya stricta has been used for decades for the treatment of diabetes mellitus and associated ailments. Considering the folkloric use of R. stricta against diabetes, it was aimed to investigate the effectiveness of its root extracts against diabetes through in vitro assays and in vivo studies using animal model along with phytochemical profiling through GCMS. Methods: Various fractions of Rhazya stricta obtained through column chromatography were evaluated for a variety of assays including a-glucosidase, Dipeptidyl peptidase-IV (DPP-IV), beta-secretase and Glucagon-like peptide-1 (GLP-1) secretion studies. For the in vivo studies the alloxan-induced diabetic mice were treated with root extracts and blood glucose levels, HbA1C, and other biochemical markers along with the histological study of the liver were done. The phytochemical identification was performed using an Agilent 7890B GC coupled to a 7010 Triple Quadrupole (MS/MS) system. GraphPad Prism software version 5.01 was used for statistical analysis. Results: Majority of the extract fractions showed excellent results against diabetes by inhibiting enzymes DPP-IV (Up to 61%) and beta-secretase (Up to 83%) with IC50s 979 pg/ml and 169 mu g/ml respectively with increase in the GLP1 secretion. The results of in vivo studies indicated a marked reduction in blood glucose and HbA1c levels along with positive effects on other parameters like lipid profile, liver functions and renal functions of extract-treated mice as compared to control. The histological examination of the liver demonstrated hepatoprotective effects against diabetes led changes and various classes of phytochemicals were also identified through GCMS in different fractions. Conclusion: The results revealed strong antidiabetic activity of R. stricta root with the potential to protect body organs against diabetic changes. Moreover, a variety of phytochemicals has also been identified through GCMS that might be responsible for the antidiabetic potential of Rhazya stricta root.
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| 13. |
- Markgren, Joel, et al.
(author)
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Clustering and cross-linking of the wheat storage protein α-gliadin : A combined experimental and theoretical approach
- 2022
-
In: International Journal of Biological Macromolecules. - : Elsevier BV. - 0141-8130 .- 1879-0003. ; 211, s. 592-615
-
Journal article (peer-reviewed)abstract
- Our aim was to understand mechanisms for clustering and cross-linking of gliadins, a wheat seed storage protein type, monomeric in native state, but incorporated in network while processed. The mechanisms were studied utilizing spectroscopy and high-performance liquid chromatography on a gliadin-rich fraction, in vitro produced alpha-gliadins, and synthetic gliadin peptides, and by coarse-grained modelling, Monte Carlo simulations and prediction algorithms. In solution, gliadins with alpha-helix structures (dip at 205 nm in CD) were primarily present as monomeric molecules and clusters of gliadins (peaks at 650- and 700-s on SE-HPLC). At drying, large polymers (Rg 90.3 nm by DLS) were formed and 13-sheets increased (14% by FTIR). Trained algorithms predicted aggregation areas at amino acids 115-140, 150-179, and 250-268, and induction of liquid-liquid phase separation at P- and Poly-Q-sequences (Score = 1). Simulations showed that gliadins formed polymers by tail-to-tail or a hydrophobic core (Kratky plots and Ree = 35 and 60 for C- and N-terminal). Thus, the N-terminal formed clusters while the C-terminal formed aggregates by disulphide and lanthionine bonds, with favoured hydrophobic clustering of similar/exact peptide sections (synthetic peptide mixtures on SE-HPLC). Mechanisms of clustering and cross-linking of the gliadins presented here, contribute ability to tailor processing results, using these proteins.
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| 14. |
- Markgren, Joel, et al.
(author)
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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
-
In: Biomolecules. - : MDPI. - 2218-273X. ; 10:8
-
Journal article (peer-reviewed)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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| 15. |
- Newson, William, et al.
(author)
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Commercial potato protein concentrate as a novel source for thermoformed bio-based plastic films with unusual polymerisation and tensile properties
- 2015
-
In: RSC Advances. - : Royal Society of Chemistry (RSC). - 2046-2069. ; 5:41, s. 32217-32226
-
Journal article (peer-reviewed)abstract
- Commercial potato protein concentrate (PPC) was investigated as a source of thermoformed bio-based plastic film. Pressing temperatures of 100 to 190°C with 15 to 25% glycerol were used to form PPC films. The shape of the tensile stress-strain curve in thermoformed PPC was controlled by glycerol level and was independent of processing temperature. Tensile testing revealed that elongation at break increased with processing temperature while Young's modulus was unaffected by processing temperature, both in contrast to previous results in protein based systems. Also in contrast to previous studies, Young's modulus was found to be only sensitive to glycerol level. Maximum tensile stress increased with increasing processing temperature for PPC films. Maximum stress and strain at break correlated with the extractable high molecular weight protein content of the processed films measured with size exclusion chromatography. Infrared absorption indicated that the content of β-sheet structure increased from the commercial protein concentrate to that pressed at 100°C, but did not further develop with increasing press temperature. Changes in structural arrangements were observed by small angle X-ray scattering indicating the development of different correlation distances with processing temperature but with no clear long range order at the supramolecular level. The novel Young's modulus behaviour appears to be due to constant secondary structure or the effect of aggregated protein structure formed during protein production. Unique strain at break behaviour with processing temperature was demonstrated, likely due to new connections formed between those aggregates.
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| 16. |
- Newson, William R., et al.
(author)
-
Commercial potato protein concentrate as a novel source for thermoformed bio-based plastic films with unusual polymerisation and tensile properties
- 2015
-
In: RSC Advances. - 2046-2069. ; 5:41, s. 32217-32226
-
Journal article (peer-reviewed)abstract
- Commercial potato protein concentrate (PPC) was investigated as a source of thermoformed bio-based plastic film. Pressing temperatures of 100 to 190 degrees C with 15 to 25% glycerol were used to form PPC films. The shape of the tensile stress-strain curve in thermoformed PPC was controlled by glycerol level and was independent of processing temperature. Tensile testing revealed that elongation at break increased with processing temperature while Young's modulus was unaffected by processing temperature, both in contrast to previous results in protein based systems. Also in contrast to previous studies, Young's modulus was found to be only sensitive to glycerol level. Maximum tensile stress increased with increasing processing temperature for PPC films. Maximum stress and strain at break correlated with the extractable high molecular weight protein content of the processed films measured with size exclusion chromatography. Infrared absorption indicated that the content of beta-sheet structure increased from the commercial protein concentrate to that pressed at 100 degrees C, but did not further develop with increasing press temperature. Changes in structural arrangements were observed by small angle X-ray scattering indicating the development of different correlation distances with processing temperature but with no clear long range order at the supramolecular level. The novel Young's modulus behaviour appears to be due to constant secondary structure or the effect of aggregated protein structure formed during protein production. Unique strain at break behaviour with processing temperature was demonstrated, likely due to new connections formed between those aggregates.
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| 17. |
- Rasheed, Faiza, et al.
(author)
-
Macromolecular changes and nano-structural arrangements in gliadin and glutenin films upon chemical modification Relation to functionality
- 2015
-
In: International Journal of Biological Macromolecules. - : Elsevier BV. - 0141-8130 .- 1879-0003. ; 79, s. 151-159
-
Journal article (peer-reviewed)abstract
- Protein macromolecules adopted for biological and bio-based material functions are known to develop a structured protein network upon chemical modification. In this study, we aimed to evaluate the impact of chemical additives such as, NaOH, NH4OH and salicylic acid (SA), on the secondary and nano-structural transitions of wheat proteins. Further, the effect of chemically induced modifications in protein macromolecular structure was anticipated in relation to functional properties. The gliadin-NH4OH-SA film showed a supramolecular protein organization into hexagonal structures with 65 angstrom lattice parameter, and other not previously observed structural entities having a characteristic distance of 50 angstrom. Proteins in gliadin-NH4OH-SA films were highly polymerized, with increased amount of disulfide crosslinks and beta-sheets, causing improved strength and stiffness. Glutenin and WG proteins with NH4OH-SA showed extensive aggregation and an increase in beta-sheet content together with irreversible crosslinks. Irreversible crosslinks hindered a high order structure formation in glutenins, and this resulted in films with only moderately improved stiffness. Thus, formation of nano-hierarchical structures based on beta-sheets and disulfide crosslinks are the major reasons of high strength and stiffness in wheat protein based films.
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| 18. |
- Rasheed, Faiza, et al.
(author)
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Mild gluten separation - A non-destructive approach to fine tune structure and mechanical behavior of wheat gluten films
- 2015
-
In: Industrial Crops and Products. - : Elsevier BV. - 0926-6690 .- 1872-633X. ; 73, s. 90-98
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Journal article (peer-reviewed)abstract
- Despite the increasing production of wheat gluten (WG) for industrial use, minor attention has been given to the impact of the separation procedure on the gluten quality. The purpose of the present study was to probe the effect of the separation treatments (harsh vs mild) on gluten structure, morphology, and performance in bio-based films. The harshly separated industrial WG showed aggregated and pre-cross linked structure in the starting material most likely due to shear forces during gluten separation from flour and heat effect during the drying procedures. Further, when the harshly separated WG was processed into films the pre-crosslinked starting material restricted new crosslinks formation and structural rearrangements at nano-scale. The mechanical integrity of the film was also affected resulting in films with low Young's modulus and strength. WG (from cultivars Diskette, Puntari, and Sleipner) recovered from mild separation showed relatively "native" non-destructed crosslinking pattern and not previously observed structural morphology at nano-scale. When processed into films the mildly separated WG showed well polymerized intimately crosslinked proteins both with disulfide and other covalent crosslinks. The nano-scale morphology showed lamellar and hexagonal arrangements, not reported so far in any study. The structural rearrangements among films from mildly separated WG resulted in materials with improved mechanical integrity as compared to films from harshly separated WG. The present study showed that the quality of WG is significantly affected by the separation procedure which also affects protein polymerization, nano-scale morphology, and tensile properties of films. (C) 2015 Elsevier B.V. All rights reserved.
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| 19. |
- Rasheed, Faiza, et al.
(author)
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Modeling to Understand Plant Protein Structure-Function Relationships-Implications for Seed Storage Proteins
- 2020
-
In: Molecules. - : MDPI. - 1431-5157 .- 1420-3049. ; 25:4
-
Research review (peer-reviewed)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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| 20. |
- Rasheed, Faiza
(author)
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Production of sustainable bioplastic materials from wheat gluten proteins
- 2011
-
Reports (other academic/artistic)abstract
- Petroleum-based products are creating a number of environmental problems. Petroleum and oil resources are also threatened to become depleted due to the massive utilization. Therefore, it is important to replace the petroleum-based products with products that are instead derived from renewable resources e.g. the replacement of petro-based plastics with bioplastics can be a good option. Wheat gluten proteins might be a promising solution to use for production of bioplastics. Wheat gluten is a cheap by-product from the bio-ethanol industry, thereby largely available and beside that, these proteins have interesting viscoelastic and thermoplastic properties. Gliadin and glutenin i.e. the two major types of gluten protein and their behavior when used to produce bio-based material are discussed in this paper.
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| 21. |
- Rasheed, Faiza, et al.
(author)
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Structural architecture and solubility of native and modified gliadin and glutenin proteins : non-crystalline molecular and atomic organization
- 2014
-
In: RSC Advances. - 2046-2069. ; 4:4, s. 2051-2060
-
Journal article (peer-reviewed)abstract
- Wheat gluten (WG) and its components, gliadin and glutenin proteins, form the largest polymers in nature, which complicates the structural architecture of these proteins. Wheat gluten, gliadin and glutenin proteins in unmodified form showed few secondary structural features. Structural modification of these proteins using heat, pressure and the chemical chaperone glycerol resulted in a shift to organized structure. In modified gliadin, nano-structural molecular arrangements in the form of hexagonal closed packed (HCP) assemblies with lattice parameter of (58 angstrom) were obvious together with development of intermolecular disulphide bonds. Modification of glutenin resulted in highly polymerized structure with proteins linked not only by disulphide bonds, but also with other covalent and irreversible bonds, as well as the highest proportion of beta-sheets. From a combination of experimental evidence and protein algorithms, we have proposed tertiary structure models of unmodified and modified gliadin and glutenin proteins. An increased understanding of gliadin and glutenin proteins structure and behavior are of utmost importance to understand the applicability of these proteins for various applications including plastic materials, foams, adhesives, films and coatings.
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| 22. |
- Rasheed, Faiza, et al.
(author)
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Structural architecture and solubility of native and modified gliadin and glutenin proteins: non-crystalline molecular and atomic organization
- 2014
-
In: RSC Advances. - : Royal Society of Chemistry (RSC). - 2046-2069. ; 4:4, s. 2051-2060
-
Journal article (peer-reviewed)abstract
- Wheat gluten (WG) and its components, gliadin and glutenin proteins, form the largest polymers in nature, which complicates the structural architecture of these proteins. Wheat gluten, gliadin and glutenin proteins in unmodified form showed few secondary structural features. Structural modification of these proteins using heat, pressure and the chemical chaperone glycerol resulted in a shift to organized structure. In modified gliadin, nano-structural molecular arrangements in the form of hexagonal closed pack (HCP) assemblies with lattice parameter of (58 Å) were obvious together with development of intermolecular disulphide bonds. Modification of glutenin resulted in highly polymerized structure with proteins linked not only by disulphide bonds, but also with other covalent and irreversible bonds, as well as the highest proportion of b-sheets. From a combination of experimental evidence and protein algorithms, we have proposed tertiary structure models of unmodified and modified gliadin and glutenin proteins. An increased understanding of gliadin and glutenin proteins structure and behavior are of utmost importance to understand the applicability of these proteins for various applications including plastics materials, foams, adhesives, films and coatings.
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| 23. |
- Rasheed, Faiza
(author)
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Tailoring the structure-function relationship in wheat gluten : processing, genotype and environment effects in bio-based materials
- 2015
-
Doctoral thesis (other academic/artistic)abstract
- Gluten proteins ranging in size from 30 000 to several million daltons form one of the largest and most complex polymers in nature. The giant molecular nature and intricate network of the over 100 types of proteins in gluten make structural studies rather challenging. This thesis examines the molecular crosslinking and structural properties of variously sourced gluten and its gliadin and glutenin protein fractions, both as unprocessed proteins and in films and foams. Protein modification through chemical additives, separation procedure and genotype (G) and environmental (E) interactions had an impact on protein polymerization, nano-structure morphology, secondary structures and the mechanical properties of films. The extent of denaturation in the starting material for film formation was of relevance for the development of specific nano-scale morphology and improved mechanical properties of films. When molded into films, non-aggregated starting material such as gliadin with additives and mildly separated gluten indicated both hydrogen- and disulfide-bonded protein network, with some non-reducible covalent crosslinks. These films also showed bi-structural morphology at nano scale. The gliadin films revealed hexagonal structures and additional not previously observed structural units. The films from mildly separated gluten also showed hexagonal and lamellar structural morphology. The films from glutenin and industrially sourced gluten proteins showed a high content of non-reducible covalent crosslinks and unorganized morphology at nano scale. The G and E interactions were associated with strong and weak gluten, resulting in films with various structural and mechanical properties. The mechanical properties of films were found to be influenced by protein structure development. Structural attributes such as relatively high number of disulfide crosslinks compared with non-reducible crosslinks, high β-sheet content and specific nano-scale morphology also led to high mechanical performance of films.
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| 24. |
- Rasheed, Faiza, et al.
(author)
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The use of plants as a "green factory" to produce high strength gluten-based materials
- 2016
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In: Green Chemistry. - : Royal Society of Chemistry. - 1463-9262 .- 1463-9270. ; 18:9, s. 2782-2792
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Journal article (peer-reviewed)abstract
- The aim of the present study was to develop an understanding of how wheat plants can be used as a "green factory" by the modulation of genotype (G) and environmental (E) interactions to fine-tune the structure and increase the strength of gluten based materials. Two wheat genotypes (5 + 10 and 2 + 12) were grown under four nitrogen and two temperature regimes to obtain gluten of various characteristics. Protein microstructure morphology revealed by confocal laser scanning microscopy suggested a higher polymerisation of proteins in glycerol plasticized films from the 5 + 10 compared to the 2 + 12 genotype. Also, films with the highest Young's modulus and maximum stress were obtained from the 5 + 10 genotype, which might be explained by the higher number of cysteine residues and consequently more disulphide crosslinks in this genotype compared to the 2 + 12 one. The presence of two nano-scaled morphologies, hexagonal and lamellar structures and their internal relations were found to be of relevance for formation of beta-sheets and also to be related to performance (strength) of the material. Thus, plants could be used as a "green factory", avoiding the use of chemicals, to tune the tensile properties of the materials. Structural properties such as relatively low protein aggregation, high beta-sheet content and a high hexagonal to lamellar structural ratio at the nano-scale were found to yield films with high stiffness and strength.
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| 25. |
- Rasheed, Faiza, et al.
(author)
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The use of plants as a “green factory” to produce high strength gluten-based materials
- 2016
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In: Green Chemistry. - 1463-9270. ; 18:9, s. 2782-2792
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Journal article (peer-reviewed)abstract
- The aim of the present study was to develop an understanding of how wheat plants can be used as a “green factory” by the modulation of genotype (G) and environmental (E) interactions to fine-tune the structure and increase the strength of gluten based materials. Two wheat genotypes (5 + 10 and 2 + 12) were grown under four nitrogen and two temperature regimes to obtain gluten of various characteristics. Protein microstructure morphology revealed by confocal laser scanning microscopy suggested a higher polymerisation of proteins in glycerol plasticized films from the 5 + 10 compared to the 2 + 12 genotype. Also, films with the highest Young’s modulus and maximum stress were obtained from the 5 + 10 genotype, which might be explained by the higher number of cysteine residues and consequently more disulphide crosslinks in this genotype compared to the 2 + 12 one. The presence of two nano-scaled morphologies, hexagonal and lamellar structures and their internal relations were found to be of relevance for formation of β-sheets and also to be related to performance (strength) of the material. Thus, plants could be used as a “green factory”, avoiding the use of chemicals, to tune the tensile properties of the materials. Structural properties such as relatively low protein aggregation, high β-sheet content and a high hexagonal to lamellar structural ratio at the nano-scale were found to yield films with high stiffness and strength.
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| 26. |
- Rasheed, Faiza, et al.
(author)
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Unraveling the Structural Puzzle of the Giant Glutenin Polymer-An Interplay between Protein Polymerization, Nanomorphology, and Functional Properties in Bioplastic Films
- 2018
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In: ACS Omega. - : AMER CHEMICAL SOC. - 2470-1343. ; 3:5, s. 5584-5592
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Journal article (peer-reviewed)abstract
- A combination of genotype, cultivation environment, and protein separation procedure was used to modify the nanoscale morphology, polymerization, and chemical structure of glutenin proteins from wheat. A low-polymerized glutenin starting material was the key to protein-protein interactions mainly via SS cross-links during film formation, resulting in extended beta-sheet structures and propensity toward the formation of nanoscale morphologies at molecular level. The properties of glutenin bioplastic films were enhanced by the selection of a genotype with a high number of cysteine residues in its chemical structure and cultivation environment with a short grain maturation period, both contributing positively to gluten strength. Thus, a combination of factors affected the structure of glutenins in bioplastic films by forming crystalline beta-sheets and propensity toward the ordered nanostructures, thereby resulting in functional properties with high strength, stiffness, and extensibility.
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| 27. |
- Sajjad, Anila, et al.
(author)
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Integration of Zinc Oxide Nanoparticles in Wheat Gluten Hydrolysates-Development of Multifunctional Films with Pliable Properties
- 2023
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In: Journal of Inorganic and Organometallic Polymers and Materials. - : Springer Nature. - 1574-1443 .- 1574-1451. ; 33:4, s. 914-929
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Journal article (peer-reviewed)abstract
- Biodegradable wheat gluten hydrolysates (WGH) and zinc oxide nanoparticles (ZNPs) with cross-linkers were prepared as nanocomposite films. The physiochemical analysis demonstrated the formation of ZNPs of size approximately 18.37 nm with spherical and hexagonal nanostructures. The ZNPs are endowed with different functional groups, as corroborated by X-ray diffractogram (XRD), field emission electron microscopy (FE-SEM), and fourier transform infrared spectroscopy (FT-IR), respectively. XRD and functional group patterns (IR) of WG and ZNPs exhibited minor changes during film development, indicating a successful interaction between the components. The SEM analysis revealed that the integration of ZNPs into the wheat gluten polymer promoted nano-aggregation on the film surface and the cross-section. The swelling capacity of films was found to be highest by WG/PVP/ZNPs with 265% (pH 7) and 198% (at pH 9). The antibacterial assessments revealed the sensitivity of Pseudomonasaeruginosa and E.coli toward WG/PVP/ZNPs with 14 and 13 mm zone of inhibition, demonstrating the maximum release of zinc ions from WG/PVP/ZNPs films. Furthermore, the WG/PVP/ZNPs film exhibits maximum oxidant scavenging (84%) and oxidant quenching potential (75%). The findings suggest that casting of WGH with ZNPs has a remarkable effect on the films’ physical and biological properties, allowing for their potential use as future bioplastics in biomedical and industrial sectors.
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| 28. |
- Sajjad, Anila, et al.
(author)
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Wheat gluten hydrolysates with embedded Ag-nanoparticles; a structure-function assessment for potential applications as wound sorbents with antimicrobial properties
- 2023
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In: Polymer testing. - : Elsevier BV. - 0142-9418 .- 1873-2348. ; 118
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Journal article (peer-reviewed)abstract
- Numerous approaches have been used to prevent bacterial infection from injured skin, such as bandages and topical creams. However, the higher level of reactive oxygen species, bacterial infections, and excess wound exudates remain the major challenges for wound healing. In this study, we have tailored the structure of wheat gluten hydrolysates (WGH) as a continuous matrix by compositing it with a minimal amount of PVA, PVP, and PEG as polymer crosslinkers (0.5 wt%) to provide film structure integrity. Silver nanoparticles (AgNPs) were impregnated into the WGH to develop a control release matrix of the AgNPs. Scanning electron microscopy, X-ray diffractogram, and functional group patterns of WG and AgNPs indicate a successful integration of AgNPs into the wheat gluten matrix. The swelling capacity of the films was tested at acidic, neutral, and basic pH and was found to be highest in WG/PEG/Ag at pH 9 with 389%. The gradual release of Ag+/AgNPs from the films significantly scavenged free radicals and increased the antibacterial activity with up to a 12 mm inhibition zone against Pseudomonas aeruginosa. According to these findings, WGH with AgNPs has been successfully cast in films with increased absorption capacity, free radicals scavenging, oxidant quenching, and antibacterial capabilities, along with the sustained release of silver ions. The results, therefore, show the potential of the developed films in biomedical applications such as wound dressing.
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