Effects of NaCl concentration and temperature on fibrillation, structure, and functional properties of soy protein isolate fibril dispersions

Ji, Fuyun; Xu, Jingjing; Ouyang, Yuanyuan; Mu, Dongdong; Li, Xingjiang; Luo, Shuhong; Shen, Yizhong; Zheng, Zhi

doi:10.1016/j.lwt.2021.111862

Cited by 48 publications

(18 citation statements)

References 40 publications

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“…Amide I band is very sensitive to changes in protein secondary structure during fibril formation [31] . The amide I band of SPI nanofibrils pretreated by ultrasound moved slightly to the smaller wavenumber, indicating that ultrasound changed the secondary structure of SPI nanofibrils [33] . The absorption peaks around 1536 cm −1 and 1539 cm −1 are associated with the amide II band (the region of 1500–1600 cm −1 ), which is mainly related to N—H bending and C—N stretching vibrations.…”

Section: Resultsmentioning

confidence: 97%

Effects of ultrasound pretreatment on functional property, antioxidant activity, and digestibility of soy protein isolate nanofibrils

2022

Ultrasonics Sonochemistry

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Section: Resultsmentioning

confidence: 97%

Effects of ultrasound pretreatment on functional property, antioxidant activity, and digestibility of soy protein isolate nanofibrils

2022

Ultrasonics Sonochemistry

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“…In addition, Lambrecht et al found that trypsinized wheat proteins formed long and straight fibrils after 40 h of heating at 85 °C [ 23 ]. Ji et al found that soy protein isolates heated at 95 °C for 1 h formed short and dispersed fibers, but after 4 h, the fibers were long and straight [ 31 ]. This suggested that worm-like oligomers were precursors to the formation of long fibers.…”

Section: Resultsmentioning

confidence: 99%

“…Thioflavin T (ThT) fluorescence was measured according to the method described by Ji et al with some modifications [ 31 ]. Briefly, 1.90 mL of the sample was mixed with 100 μL of 200 μM ThT in a dark room for 1 h. Next, the sample was detected using an F-7100 fluorescence spectrophotometer (Hitachi, Tokyo, Japan) with excitation wavelengths at 440 nm and emission wavelengths from 460 to 600 nm.…”

Section: Methodsmentioning

confidence: 99%

Effect of Thermal Treatment on the Self-Assembly of Wheat Gluten Polypeptide

et al. 2023

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Self-assembled fibrillation of wheat gluten is a common phenomenon in the daily production and processing of wheat flour products. The driving forces for its formation and the factors that influence the morphology of fibrils have not been thoroughly investigated. In this study, the effect of three bonding changes (breaking hydrogen bonds, strengthening hydrophobic interactions, and SH-SS exchange reactions) on gluten polypeptide (GP) fibrillation was simulated by adjusting the heating temperature (room temperature (RT), 45 °C, 65 °C, and 95 °C). The results showed that the breakage of hydrogen bonds could induce conformational transitions in GPs and help to excite fibrillation in GPs. Strengthened hydrophobic interactions significantly contributed to the fibrillation of GPs. Covalent crosslinks generated by SH-SS exchange reactions might also promote the fibrillation of GPs. GPs with different degrees of hydrolysis (4.0%, 6.0%, and 10.0%, represented by DH 4, DH 6, and DH 10, respectively) presented different extents of fibrillation, with DH 10 GPs having a higher propensity to fibrillation than DH 4 and DH 6 GPs. The results of Fourier’s transform infrared spectroscopy indicated that hydrophobic interactions drive the transition from a random coil and α-helix to a β-sheet. In addition, hydrophobic interactions also drive the intermolecular polymerization of GPs, resulting in larger molecular weight aggregates. The morphology presented by transmission electron microscopy showed that the greater the DH, the stronger the tendency for the worm-like aggregation of GPs.

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“…The pea protein fibrils were generally straighter and similar to fibrils formed by lysozyme and β-lactoglobulin, while soy protein fibrils (crude protein extract and 7S-enriched) were mainly worm-like , The fibril morphologies observed here are largely consistent with other investigations of pea and soy protein extracts, soy β-conglycinin, and glycinin, except that the straight glycinin and pea protein fibrils observed here were not reported previously. ,, Although multiple factors were found to affect fibril morphology (stirring, protein concentration, ionic strength, etc. ), the underlying rationale is not fully understood. − We discovered that under the same condition, 7S and 11S globulins enriched from the same crude protein extracts might generate morphologically homogeneous or heterogeneous fibrils. The shorter, fewer fibrils found in the samples at 78 h are in line with the results of the ThT assay and confirmed the fibril fragmentation from around 30–78 h. , The ThT fluorescence intensity may indicate a relative fibril concentration (as shown in pea 7S globulin and soy crude protein extract, which also displayed the highest and lowest fibril density, respectively, in TEM images) but does not necessarily reflect the fibrillation stage.…”

Section: Resultsmentioning

confidence: 99%

Morphology, Formation Kinetics and Core Composition of Pea and Soy 7S and 11S Globulin Amyloid Fibrils

Zhang

Dee

2023

J. Agric. Food Chem.

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Legume seed storage proteins can be induced to form amyloid fibrils upon heating at low pH, which could improve their functionality for use in food and materials. However, the amyloidogenic regions of legume proteins are largely unknown. Here, we used LC-MS/MS to determine the amyloid core regions of fibrils formed by enriched pea and soy 7S and 11S globulins at pH 2, 80 °C, and characterized their hydrolysis, assembly kinetics, and morphology. A lag phase was absent from the fibrillation kinetics of pea and soy 7S globulins, while 11S globulins and crude extracts displayed a similar lag time. Pea and soy protein fibrils differed in morphology, with most pea fibrils being straight and soy fibrils being worm-like. Pea and soy globulins were abundant in amyloidforming peptides, with over 100 unique fibril-core peptides from pea 7S and around 50 unique fibril-core peptides identified from pea 11S, soy 7S, and soy 11S globulins. Amyloidogenic regions derive predominantly from the homologous core region of 7S globulins and the basic subunit of 11S globulins. Overall, pea and soy 7S and 11S globulins are rich in amyloidogenic regions. This study will help understand their fibrillation mechanism and engineer protein fibrils with specific structures and functionality.

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Effects of NaCl concentration and temperature on fibrillation, structure, and functional properties of soy protein isolate fibril dispersions

Cited by 48 publications

References 40 publications

Effects of ultrasound pretreatment on functional property, antioxidant activity, and digestibility of soy protein isolate nanofibrils

Effects of ultrasound pretreatment on functional property, antioxidant activity, and digestibility of soy protein isolate nanofibrils

Effect of Thermal Treatment on the Self-Assembly of Wheat Gluten Polypeptide

Morphology, Formation Kinetics and Core Composition of Pea and Soy 7S and 11S Globulin Amyloid Fibrils

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