Conformation of the Z19 Prolamin by FTIR, NMR, and SAXS

Forato, L. A.; Doriguetto, Antônio C.; Fischer, Hannes; Mascarenhas, Yvonne P.; Craievich, Aldo Felix; Colnago, Luiz Alberto

doi:10.1021/jf035020+

Cited by 58 publications

(70 citation statements)

References 13 publications

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“…The polypeptide monomers are, however, all much smaller in size than the wheat HMW-GS, but like the HMW-GS they polymerise through disulphide cross-linking, due to the high cysteine content of the β-and γ-sub-classes. The secondary structures of zein and kafirin are predominately α-helical and tightly folded into a hairpin or rod-like structure , rather than consisting of more open , 1982;Tatham et al, 1993, Forato et al, 2004, Cabra et al, 2005) 7-19.5% β-sheet (Cabra et al, 2005. Classic Argos model based on 9 anti-parallel α-helices within a distorted cylinder (Argos et al, 1982).…”

Section: Composition and Structure Of The Storage Proteins Of Non-whementioning

confidence: 99%

“…Classic Argos model based on 9 anti-parallel α-helices within a distorted cylinder (Argos et al, 1982). Modified models based on extended hairpin, rod or ribbonlike structures 17 x 4.5 x 1.2 nm, with clearly defined hydrophilic and hydrophobic domains (Matsushima et al, 1997;Bugs et al, 2004;Forato et al, 2004;Momany et al, 2006) Mainly β-sheet, β-turn and random coil (Shewry and Tatham, 1990). No structural model.…”

Section: Composition and Structure Of The Storage Proteins Of Non-whementioning

confidence: 99%

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Functionality of the storage proteins in gluten-free cereals and pseudocereals in dough systems

Taylor

Campanella

et al. 2016

Journal of Cereal Science

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The dough functionality of the storage proteins in "gluten-free" grains has been studied for almost 25 years. Zein, maize prolamin, when isolated as α-zein can form a wheat gluten-like visco-elastic dough when mixed with water above its glass transition temperature. There is good evidence that its dough-forming properties are related to a change in protein conformation from α-helix to β-sheet and association of the molecules into fibrils. Stabilisation of β-sheet structure and visco-elasticity can be enhanced by inclusion of a co-protein. No other isolated cereal or pseudocereal storage protein has been shown to form a visco-elastic dough. Many treatments have been applied to improve "gluten-free" storage protein functionality, including acid/base, deamidation, cross-linking by oxidising agents and transglutaminase, proteolysis, disulphide bond reduction and high pressure treatment. Such treatments have some limited positive benefits on batter-type dough functionality, but none is universally effective and the effects seem to be dependent on the composition and structure of the particular storage protein. Research into mutants where prolamin synthesis is altered appears to be promising in terms of improved dough functionality and scientific understanding. Research into how treatments affect the functionality and structure of isolated storage proteins from "gluten-free" grains other than maize is required.2

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Section: Composition and Structure Of The Storage Proteins Of Non-whementioning

confidence: 99%

Section: Composition and Structure Of The Storage Proteins Of Non-whementioning

confidence: 99%

Functionality of the storage proteins in gluten-free cereals and pseudocereals in dough systems

Taylor

Campanella

et al. 2016

Journal of Cereal Science

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“…Several models have been proposed for the 3D shape of α-zein (Argus et al, 1982;Garrett et al, 1993;Tatham et al, 1993;Matsushima et al, 1997;Bugs et al, 2004;Forato et al, 2004). Despite all these trials, a generally accepted axial ratio of the individual molecule has not even been obtained yet.…”

Section: Future Researchmentioning

confidence: 99%

Production of biopolymer composites by particle bonding

Kim¹,

Xu²,

Liu³

2010

Composites Part A: Applied Science and Manufacturing

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“…The secondary structure of a-zein dissolved in 70% aqueous ethanol or methanol has been shown to range from 40-60% a-helical (Argos et al 1982;Cabra et al 2005;Forato et al 2004;Tatham et al 1993) and between 7.1 and 19.5% β-sheet (Cabra et al 2005), whereas, Z19-zein, studied by Fourier transform infrared spectroscopy (FTIR) in the solid state showed 46% a-helix and 22% β-sheet . One of the earliest models for a-zein is based on a group of nine anti-parallel (hairpin) a-helices arranged within a distorted cylinder (Argos et al 1982).…”

mentioning

confidence: 99%

“…Physical data suggested that a-zeins were present in solution as extended structures (Tatham et al 1993). Subsequently, a number of other models have been proposed many of them based on extended helical hairpin, rod or ribbon type structures 17 nm in length, 4.5 nm wide and 1.2 nm thick with clearly defined hydrophilic and hydrophobic domains (Matsushima et al 1997, Bugs et al 2004Forato et al 2004;Momany et al 2006).…”

mentioning

confidence: 99%

Developments in the Science of Zein, Kafirin, and Gluten Protein Bioplastic Materials

Anyango

Taylor

2013

Cereal Chem

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Despite much research, there are very few commercial prolamin bio-plastics. The major reason, apart from their high cost, is that they have inferior functional properties compared to synthetic polymer plastics. This is because the prolamins are complex, each consisting of several classes and sub-classes and the functional properties of their bio-plastics are greatly affected by water. Prolamin bio-plastics are produced by protein aggregation from a solvent or by thermoplastic processing. Recent research indicates that protein aggregation occurs by polypeptide self-assembly into nanostructures. Protein secondary structure in terms of α-helical and β-sheet structure seems to play a key, but incompletely understood role in assembly. Also, there is inadequate knowledge as to how these nanostructures further assemble and organize into the various forms of prolamin bio-plastics such as films, fibres, microparticles and scaffolds. Some improvements in bio-plastic functionality have been made by better prolamin solvation, plasticization, physical and chemical cross-linking, derivatization and blending with other polymers. The most promising area of 2 commercialization is the biomedical field where the relative hydrophilicity, compatibility and biodegradability of particularly zein and kafirin are advantageous. With regard to biomedical applications, "supramolecular design" of prolamin bio-plastics through control over interand intramolecular weak interactions and SS/SH interchange between and within polypeptides appears to have considerable potential.

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Conformation of the Z19 Prolamin by FTIR, NMR, and SAXS

Cited by 58 publications

References 13 publications

Functionality of the storage proteins in gluten-free cereals and pseudocereals in dough systems

Functionality of the storage proteins in gluten-free cereals and pseudocereals in dough systems

Production of biopolymer composites by particle bonding

Developments in the Science of Zein, Kafirin, and Gluten Protein Bioplastic Materials

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