Effects of Physical and Chemical Factors on the Structure of Gluten, Gliadins and Glutenins as Studied with Spectroscopic Methods

Kłosok, Konrad; Welc, Renata; Fornal, Emilia; Nawrocka, Agnieszka

doi:10.3390/molecules26020508

Cited by 50 publications

(15 citation statements)

References 129 publications

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“…High and low molecular subunits of glutenins were connected via covalent SS bonds. However, glutenins and gliadins interacted mainly via hydrogen or non-covalent bonds [ 24 , 54 , 55 ].…”

Section: Discussionmentioning

confidence: 99%

Does Nitrogen Fertilization Affect the Secondary Structures of Gliadin Proteins in Hypoallergenic Wheat?

et al. 2022

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One of the macronutrients indispensable for plant growth and development is nitrogen (N). It is responsible for starch and storage protein (gliadins and glutenins) biosynthesis and, in consequence, influences kernels’ quality and yields. However, applying N-fertilizers increases gluten content in wheat, and it may intensify the risk of developing allergy symptoms in gluten-sensitive individuals. The purpose of our research was to analyse whether and how the elimination of N-fertilizers during the cultivation of wasko.gl− wheat (modified genotype lacking ω-gliadins) changes the secondary structures of gliadin proteins. To this aim, using the FT-Raman technique, we examined flour and gliadin protein extracts obtained from kernels of two winter wheat lines: wasko.gl+ (with a full set of gliadin proteins) and wasko.gl− (without ω-gliadin fraction) cultivated on two different N-fertilization levels—0 and 120 kg N·ha−1. On the basis of the obtained results, we proved that nitrogen fertilization does not have a major impact on the stability of the secondary structures of gliadin proteins for wasko.gl− wheat line with reduced allergenic properties. Furthermore, the results presented herein suggest the possibility of increasing the stability of glutenin structures as a result of the N-fertilization of wasko.gl− wheat line, which gives hope for its use in the production of wheat articles devoted to people suffering from diseases related to gluten sensitivity.

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“…High and low molecular subunits of glutenins were connected via covalent SS bonds. However, glutenins and gliadins interacted mainly via hydrogen or non-covalent bonds [ 24 , 54 , 55 ].…”

Section: Discussionmentioning

confidence: 99%

Does Nitrogen Fertilization Affect the Secondary Structures of Gliadin Proteins in Hypoallergenic Wheat?

et al. 2022

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“…On the other hand, cysteines present in both prolamin groups connect with each other via highly energetic disulfide bonds (SS), which play an important role in the stabilization of protein higher-order structures. Gliadins are able to form mainly intramolecular, while glutenins form mainly intermolecular disulfide bonds [ 30 , 31 ]. However, there is one exception—both subgroups of ω-gliadins are completely devoid of cysteine residues [ 32 ].…”

Section: Introductionmentioning

confidence: 99%

FT-Raman Spectroscopy as a Tool to Study the Secondary Structures of Wheat Gliadin Proteins

et al. 2021

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Raman spectroscopy is a useful method in biological, biomedical, food, and agricultural studies, allowing the simultaneous examination of various chemical compounds and evaluation of molecular changes occurring in tested objects. The purpose of our research was to explain how the elimination of ω-fractions from the wheat gliadin complex influences the secondary structures of the remaining αβγ-gliadins. To this aim, we analyzed the endosperm of wheat kernels as well as gliadin proteins extracted from two winter wheat genotypes: wasko.gl+ (control genotype containing the full set of gliadins) and wasko.gl− (modified genotype lacking all ω-gliadins). Based on the decomposition of the amide I band, we observed a moderate increase in β-forms (sheets and turns) at the expense of α-helical and random coil structures for gliadins isolated from the flour of the wasko.gl− line. Since ω-gliadins contain no cysteine residues, they do not participate in the formation of the disulfide bridges that stabilize the protein structure. However, they can interact with other proteins via weak, low-energetic hydrogen bonds. We conclude that the elimination of ω-fractions from the gliadin complex causes minor modifications in secondary structures of the remaining gliadin proteins. In our opinion, these small, structural changes of proteins may lead to alterations in gliadin allergenicity.

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“…The ratio of these band intensities I(850)/I(830) (tyrosine doublet) is used as an indicator of hydrogen bonding of the phenolic hydroxyl groups. A decrease in the tyrosine doublet shows the burriedness of tyrosine residues with the formation of intramolecular hydrogen bonds, and an increase indicates exposition of the residues on the surface of the protein complex [34]. In our research, for sonicated samples, the tyrosine doublet was higher than for unsonicated gluten (0.96 and 0.89, respectively), which indicates exposition of the tyrosine residues on the surface of the protein complex.…”

Section: Infrared Attenuated Total Reflectance (Ir-atr) Spectroscopymentioning

confidence: 39%

Influence of Farming System and Forecrops of Spring Wheat on Protein Content in the Grain and the Physicochemical Properties of Unsonicated and Sonicated Gluten

et al. 2022

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The potential for enhancing the spring wheat protein content by different cultivation strategies was explored. The influence of ultrasound on the surface and rheological properties of wheat-gluten was also studied. Spring wheat was cultivated over the period of 2018–2020 using two farming systems (conventional and organic) and five forecrops (sugar beet, spring barley, red clover, winter wheat, or oat). The obtained gluten was sonicated using the ultrasonic scrubber. For all organically grown wheat, the protein content was higher than for the conventional one. There was no correlation between the rheological properties of gluten and the protein content in the grain. Gluten derived from organically grown wheat was more elastic than those derived from the conventional one. Sonication enhanced the elasticity of gluten. The sonication effect was influenced by the forecrops. The most elastic gluten after sonication was found for organic barley and sugar beet. The lowest values of tan (delta) were noted for conventional wheat and conventional oat. Cultivation in the monoculture gave gluten with a smaller susceptibility to increase elasticity after sonic treatment. Sonication promoted the cross-linking of protein molecules and induced a more hydrophobic character, which was confirmed by an increment in contact angles (CAs). Most of the organically grown wheat samples showed a lower CA than the conventional ones, which indicated a less hydrophobic character. The gluten surface became rougher with the sonication, regardless of the farming system and applied forecrops. Sonication treatment of gluten proteins rearranged the intermolecular linkages, especially disulfide and hydrophobic bonds, leading to changes in their surface morphology.

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Effects of Physical and Chemical Factors on the Structure of Gluten, Gliadins and Glutenins as Studied with Spectroscopic Methods

Cited by 50 publications

References 129 publications

Does Nitrogen Fertilization Affect the Secondary Structures of Gliadin Proteins in Hypoallergenic Wheat?

Does Nitrogen Fertilization Affect the Secondary Structures of Gliadin Proteins in Hypoallergenic Wheat?

FT-Raman Spectroscopy as a Tool to Study the Secondary Structures of Wheat Gliadin Proteins

Influence of Farming System and Forecrops of Spring Wheat on Protein Content in the Grain and the Physicochemical Properties of Unsonicated and Sonicated Gluten

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