Vibrational and fluorescence spectroscopy to study gluten and zein interactions in complex dough systems

Sadat, Azin; Corradini, Maria G.; Joye, Iris J.

doi:10.1016/j.crfs.2022.02.009

Cited by 14 publications

(7 citation statements)

References 66 publications

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“…The final simulation snapshots at 375 ns for three simulation replicates in Fig 17 D - I show non-covalent zein aggregates with both branching and linear features, resembling fractal-like aggregates [84]. The aggregates appear consistent with the known capacity of α-zeins to form viscoelastic networks in zein dough systems [85], even though the simulated structures lack β-sheets, which are presumed to have a central role in dough formation [86]. A notable limitation of the coarse-grained simulations is that the initial secondary structure assignment remains fixed throughout the simulations.…”

Section: Resultsmentioning

confidence: 93%

Conformations of a highly expressed Z19 α-zein studied with AlphaFold2 and MD simulations

Christensen

2023

Preprint

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Alpha-zeins are amphiphilic maize proteins with interesting material properties suitable for numerous applications, e.g., in renewable plastics, foods, therapeutics and additive manufacturing (3D-printing). To exploit their full potential, molecular-level insights are essential. Since alpha-zeins have resisted experimental atomic-resolution characterization, molecular models have been central to elucidating their structure, but deep-learning alpha-zein models are largely unexplored. Therefore, this work studies an AlphaFold2 model of a highly expressed zein with molecular dynamics (MD) simulations. The mature protein sequence of the alpha-zein cZ19C2 gave a loosely packed model with 7 alpha-helical segments connected by turns/loops and 68% total alpha-helicity. Compact tertiary structure was limited to a C-terminal bundle of three alpha-helices, each aligning well with the published repeat sequence NPAAYLQQQQLLPFNQLA(V/A)(L/A). The model was subjected to MD simulations in water containing 0, 3, 23, 50, and 100 mol% ethanol for 400 ns, with extension of selected simulations to the us timescale. Although the simulations gave structurally diverse endpoints, several patterns were observed: In water and less than or equal to 2 mol% ethanol, the model rapidly formed compact globular structures, largely preserving the C-terminal bundle. At greater than or equal to 50 mol% ethanol, extended conformations prevailed, consistent with previous SAXS studies. Tertiary structure was partially stabilized in water and in 2 mol% and 23 mol% ethanol, but was disrupted in greater than or equal to 50 mol% ethanol. Averaged results indicated slightly increased helicity with ethanol concentration. Multiple copies of a globular model conformation rapidly formed branched aggregates in aqueous all-atom and coarse-grained MD simulations. Beta-sheet content was typically <1% across all simulations. In aqueous simulations with glycidyl methacrylate (GMA), 55% of GMA was found within 4 Angstrom of the model. Pre-reaction complexes for methacrylation were indicated by GMA epoxide carbons within 2.9 - 3.3 Angstrom of side chain hydroxyl oxygens, suggesting accessibility of reactive sites in compact alpha-zein conformations.

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Section: Resultsmentioning

confidence: 93%

Conformations of a highly expressed Z19 α-zein studied with AlphaFold2 and MD simulations

Christensen

2023

Preprint

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“…All fluorescence intensities were corrected based on a previously reported method to remove internal filtering effects. 21,22 The quenching mechanism was determined using the Stern–Volmer eqn (1), as follows: 23 F 0 / F = 1 + K SV [ Q ]where F and F 0 are the fluorescence intensities of lipase with different concentrations of HYP and free lipase, respectively. K SV is the Stern–Volmer quenching constant, and [ Q ] is the HYP concentration.…”

Section: Methodsmentioning

confidence: 99%

“…All uorescence intensities were corrected based on a previously reported method to remove internal ltering effects. 21,22 The quenching mechanism was determined using the Stern-Volmer eqn (1), as follows: 23…”

Section: Fluorescence Titration Measurementsmentioning

confidence: 99%

Exploring the binding effects and inhibiting mechanism of hyperoside to lipase using multi-spectroscopic approaches, isothermal titration calorimetry, inhibition kinetics and molecular dynamics

Zeng

Tang

et al. 2023

RSC Adv.

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“…The I 850 /I 830 value of NG foams at pH 4.0 was 0.84 which was slightly higher than the value obtained for NG foams at pH 6.0 (0.80). This suggests that in NG, the Tyr ring was buried inside the protein structure at both pH 4.0 and 6.0, implying that the Tyr ring was involved in hydrogen bonds within the protein and particle structure (Sadat et al, 2022).…”

Section: Changes In Tyr Environmentmentioning

confidence: 99%

Impact of deamidation on the physicochemical properties and air-water interfacial behaviour of gliadin nanoparticles

Moraveji

Sadat

Joye

2022

Front. Soft. Matter

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Gliadin due to its low water solubility is excellently suited to make biopolymeric nanoparticles through liquid antisolvent precipitation. These gliadin nanoparticles (GNPs) can be utilized to populate and stabilize interfaces. Gliadin, by nature a protein that carries a low charge, can be altered by deamidation. Deamidation effectively alters the physicochemical properties of gliadin through decreasing the protein’s isoelectric point (IEP). The objective of this study is to explore the effect of different degrees of deamidation on gliadin nanoparticle (interfacial) characteristics. Besides altering the physical stability of GNP suspensions, deamidation did alter the functionality of GNPs as interfacial agents. GNP behaviour at the air-water interface is substantially impacted by pH. Particles made with untreated and deamidated gliadin exhibited a greater tendency to adsorb and form strong viscoelastic films at the air-water interface and better foam structures closer to their IEP. The combination of SEM, confocal Raman microscopy and drop tensiometry provides unique insights in the dominant gliadin structures and interactions at the interfacial film. This study provides crucial insights into the potential of deamidation to tailor gliadin and GNP properties for specific food applications.

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Vibrational and fluorescence spectroscopy to study gluten and zein interactions in complex dough systems

Cited by 14 publications

References 66 publications

Conformations of a highly expressed Z19 α-zein studied with AlphaFold2 and MD simulations

Conformations of a highly expressed Z19 α-zein studied with AlphaFold2 and MD simulations

Exploring the binding effects and inhibiting mechanism of hyperoside to lipase using multi-spectroscopic approaches, isothermal titration calorimetry, inhibition kinetics and molecular dynamics

Impact of deamidation on the physicochemical properties and air-water interfacial behaviour of gliadin nanoparticles

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