Conformational Change in a Single Molecular Species, β<sub>3</sub>, of β-Conglycinin in Acidic Ethanol Solution

Tsumura, Kyosuke; Enatsu, Makoto; Kuramori, Koichi; Morita, Shimpei; Kugimiya, Wataru; Kuwada, Masahiro; Shimura, Yuki; Hasumi, Hideyo

doi:10.1271/bbb.65.292

Cited by 14 publications

(6 citation statements)

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“…for 5× desolvation, 48.8% α-helices at pH 3 versus 35.6% at pH 10. This finding is in agreement with the report of Tsumura et al [31], who investigated the changes in secondary structures of soybean β-conglycinin using far-UV circular dichroism. The quantity of β-turn also showed an increase with ethanol desolvation ratio at pH 3.…”

Section: Resultssupporting

confidence: 93%

“…After removal of more hydrophobic insoluble components, the average secondary structure of the supernatant (PPS) at pH 10 showed an increase in β-sheets and α-helices, while β-turns decreased and no RC was found. Acidification of the supernatant PPS (pH 3) caused a significant increase in α-helices at the expense of β-sheets and β-turns structures, which could be due to the neutralization of acidic amino acids by protonation, resulting in a decrease in negative charge and formation of more local hydrogen bonded α-helical structures [31].…”

Section: Resultsmentioning

confidence: 99%

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Formation and Stability of Pea Proteins Nanoparticles Using Ethanol-Induced Desolvation

Doan

Ghosh

2019

Nanomaterials

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Protein nanoparticles have recently found a lot of interests due to their unique physicochemical properties and structure-functionality compared to the conventional proteins. The aim of this research was to synthesize pea protein nanoparticles (PPN) using ethanol-induced desolvation, to determine the changes in secondary structures and the particle stability in an aqueous dispersion. The nanoparticles were prepared by diluting 3.0 wt% pea protein solutions in 1–5 times ethanol at pH 3 and 10 at different temperatures. Higher ratios of ethanol caused greater extent of desolvation and larger sizes of PPN. After homogenization at 5000 psi for 5 min, PPN displayed uniform size distribution with a smaller size and higher zeta potential at pH 10 compared to pH 3. PPN prepared from a preliminary thermal treatment at 95 °C revealed a smaller size than those synthesized at 25 °C. Electron microscopy showed roughly spherical shape and extensively aggregated state of the nanoparticles. Addition of ethanol caused a reduction in β-sheets and an increase in α-helices and random coil structures of the proteins. When PPN were separated from ethanol and re-dispersed in deionized water (pH 7), they were stable over four weeks, although some solubilization of proteins leading to a loss in particle size was observed.

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Section: Resultssupporting

confidence: 93%

Section: Resultsmentioning

confidence: 99%

Formation and Stability of Pea Proteins Nanoparticles Using Ethanol-Induced Desolvation

Doan

Ghosh

2019

Nanomaterials

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“…The changes in these two regions may be attributed to the hydroxyl groups of the carbohydrate fraction possibly involved in hydrogen bonding (1041 cm -1 ) as well as to those interacting with the protein component. 27 In both soybean flour and SB, the occurrence of inter-and intramolecular hydrogen bonds is also confirmed by the broad absorption band observed in the frequency range 3600-3000 cm -1 . This signal was attributed to free and bound O-H and N-H groups and appeared to be broader in SB.…”

Section: Resultsmentioning

confidence: 78%

A New Class of Bioactive and Biodegradable Soybean-Based Bone Fillers

et al. 2007

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The reconstruction of large bone defects in periodontal, maxillofacial, and orthopedic surgery relies on the implantation of biomaterials able to support the growth of new tissue. None of the materials currently available is able to combine all the properties required, which are (i) easy handling, (ii) biodegradation, (iii) low immunogenicity, and more importantly, (iv) induction of tissue regeneration. A new class of biodegradable biomaterials has been obtained by simple thermosetting of defatted soybean curd. The final material can be processed into films, porous scaffolds, and granules for different surgical needs. When incubated in physiological solutions the material shows water uptake of 80%, elongation at break of 0.9 mm/mm, and 25% (w/w) degradation in 7 days. Soybean-based biomaterial granules are shown to reduce the activity of the monocytes/macrophages and of the osteoclasts and to induce osteoblast differentiation in vitro, thus demonstrating a bone regeneration potential suitable for many clinical applications.

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“…Using thermal analysis, the loss of denaturation enthalpy value (Δ H ) of β-conglycinin (94.8%) is higher than that of glycinin (48.1%) during SPC preparation . Conformational transitions of both β-conglycinin and glycinin to α-helix structure occur during EtOH treatment at acidic and alkaline pH. , In fact, different from heat denaturation, EtOH is generally considered to weaken noncovalent bonds in protein, and simultaneously to enhance local hydrogen bonds because of its lower dielectric coefficient. , Thus, the formation of an α-helical conformation appears to be a generic alcohol-denatured behavior for many globulin proteins . Moreover, the exposure of hydrophobic side chains and the burying of polar amide groups through the formation of helix structure may be the reasons for the insolubility of EtOH-denatured proteins …”

Section: Introductionmentioning

confidence: 99%

“…3 Conformational transitions of both β-conglycinin and glycinin to R-helix structure occur during EtOH treatment at acidic and alkaline pH. 4,5 In fact, different from heat denaturation, EtOH is generally considered to weaken noncovalent bonds in protein, and simultaneously to enhance local hydrogen bonds because of its lower dielectric coefficient. 6,7 Thus, the formation of an R-helical conformation appears to be a generic alcohol-denatured behavior for many globulin proteins.…”

Section: ' Introductionmentioning

confidence: 99%

Structural Rearrangement of Ethanol-Denatured Soy Proteins by High Hydrostatic Pressure Treatment

Wang

Yang

Yin

et al. 2011

J. Agric. Food Chem.

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The effects of high hydrostatic pressure (HHP) treatment (100-500 MPa) on solubility and structural properties of ethanol (EtOH)-denatured soy β-conglycinin and glycinin were investigated using differential scanning calorimetry, Fourier transform infrared and ultraviolet spectroscopy. HHP treatment above 200 MPa, especially at neutral and alkaline pH as well as low ionic strength, significantly improved the solubility of denatured soy proteins. Structural rearrangements of denatured β-conglycinin subjected to high pressure were confirmed, as evidenced by the increase in enthalpy value (ΔH) and the formation of the ordered supramolecular structure with stronger intramolecular hydrogen bond. HHP treatment (200-400 MPa) caused an increase in surface hydrophobicity (F(max)) of β-conglycinin, partially attributable to the exposure of the Tyr and Phe residues, whereas higher pressure (500 MPa) induced the decrease in F(max) due to hydrophobic rearrangements. The Trp residues in β-conglycinin gradually transferred into a hydrophobic environment, which might further support the finding of structural rearrangements. In contrast, increasing pressure induced the progressive unfolding of denatured glycinin, accompanied by the movement of the Tyr and Phe residues to the molecular surface of protein. These results suggested that EtOH-denatured β-conglycinin and glycinin were involved in different pathways of structural changes during HHP treatment.

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Conformational Change in a Single Molecular Species, β₃, of β-Conglycinin in Acidic Ethanol Solution

Cited by 14 publications

References 1 publication

Formation and Stability of Pea Proteins Nanoparticles Using Ethanol-Induced Desolvation

Formation and Stability of Pea Proteins Nanoparticles Using Ethanol-Induced Desolvation

A New Class of Bioactive and Biodegradable Soybean-Based Bone Fillers

Structural Rearrangement of Ethanol-Denatured Soy Proteins by High Hydrostatic Pressure Treatment

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Conformational Change in a Single Molecular Species, β3, of β-Conglycinin in Acidic Ethanol Solution

Cited by 14 publications

References 1 publication

Formation and Stability of Pea Proteins Nanoparticles Using Ethanol-Induced Desolvation

Formation and Stability of Pea Proteins Nanoparticles Using Ethanol-Induced Desolvation

A New Class of Bioactive and Biodegradable Soybean-Based Bone Fillers

Structural Rearrangement of Ethanol-Denatured Soy Proteins by High Hydrostatic Pressure Treatment

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Product

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Conformational Change in a Single Molecular Species, β₃, of β-Conglycinin in Acidic Ethanol Solution