Formation and pH-stability of whey protein fibrils in the presence of lecithin

Mantovani, Raphaela Araújo; Fattori, Juliana; Michelon, Mariano; Cunha, Rosiane L.

doi:10.1016/j.foodhyd.2016.03.039

Cited by 94 publications

(33 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The content of the secondary structures were calculated and listed in Table 1. A broad depression with a minimum plateau from 208 to 222 nm and a zero crossing around 203 nm, suggesting the predominant secondary structure conformation of α-helix and β-sheet could be observed from WP and WP-SL samples (Taheri-Kafrani et al, 2010). Similar result was reported by Mantovani et al (2016). Protein unfolding as a consequence of WP and Figure 6.…”

Section: Secondary Structure Of Wp or Pwp In The Presence Of Slsupporting

confidence: 75%

“…The content of secondary structures including α-helix, β-strands, β-turns, and random coil were calculated using CONTIN (DichroWeb; http: / / dichroweb .cryst .bbk .ac .uk/ html/ home .shtml), which fits the CD of unknown proteins by a linear combination of the spectra using a large database of proteins with known conformations (Chandrapala et al, 2011). Mean residue weight was estimated as 114 Da based on the molecular masses of the 3 major components: β-LG, α-LA, and BSA (Mantovani et al, 2016).…”

Section: Far-uv Circular Dichroism Spectrummentioning

confidence: 99%

See 1 more Smart Citation

Interactions between whey protein or polymerized whey protein and soybean lecithin in model system

Sun

Wang

Guo

2018

Journal of Dairy Science

View full text Add to dashboard Cite

Soybean lecithin is often used as a surfactant in food formulation. The aim of this study was to investigate the interactions between soybean lecithin (SL, 0-3%, wt/vol) and whey protein (WP, 10%, wt/vol) or polymerized whey protein (PWP, 10%, wt/vol) induced by heating WP solutions at 85°C for 0 to 20 min at pH 7.0. The samples were evaluated for zeta potential, particle size, morphology, rheological properties, thermal properties, secondary structure, and surface hydrophobicity. Zeta potential of WP increased linearly as SL level increased from 0 to 3%, whereas that of PWP changed with plateau at SL level of 1%, which may be due to the aggregation of SL. The addition of SL increased the particle size and apparent viscosity of both WP and PWP. All the samples exhibited different morphology depending on SL level and heating time according to transmission electron microscopy images. Whey protein showed obviously decreased gelation time and increased storage modulus in the presence of SL. Differential scanning calorimetry curves confirmed the effects of SL on the thermal properties of both WP and PWP. Circular dichroism spectra indicated that SL had effects on the secondary structure of both WP and PWP. The changes in surface hydrophobicity indicated the hydrophobic interactions between WP/PWP and SL. Data indicate that the physicochemical and functional properties of WP and PWP can be altered by adding soybean lecithin.

show abstract

Section: Secondary Structure Of Wp or Pwp In The Presence Of Slsupporting

confidence: 75%

Section: Far-uv Circular Dichroism Spectrummentioning

confidence: 99%

Interactions between whey protein or polymerized whey protein and soybean lecithin in model system

Sun

Wang

Guo

2018

Journal of Dairy Science

View full text Add to dashboard Cite

show abstract

“…This result might be attributed to the interaction between zein and lecithin. Mantovani, Fattori, Michelon, & Cunha [31] also observed that mixing soy lecithin to whey protein led to an increase in α-helix content from 20 to 23% and a decrease in β-strand content from 26 to 24%. This transition from native β-structure to non-native α-helical structure was a consequence of the protein-soy lecithin phospholipids interaction.…”

Section: Resultsmentioning

confidence: 99%

The Interaction between Zein and Lecithin in Ethanol-Water Solution and Characterization of Zein–Lecithin Composite Colloidal Nanoparticles

Dai¹,

Sun²,

Wang³

et al. 2016

PLoS ONE

110

View full text Add to dashboard Cite

Lecithin, a naturally small molecular surfactant, which is widely used in the food industry, can delay aging, enhance memory, prevent and treat diabetes. The interaction between zein and soy lecithin with different mass ratios (20:1, 10:1, 5:1, 3:1, 2:1, 1:1 and 1:2) in ethanol-water solution and characterisation of zein and lecithin composite colloidal nanoparticles prepared by antisolvent co-precipitation method were investigated. The mean size of zein-lecithin composite colloidal nanoparticles was firstly increased with the rise of lecithin concentration and then siginificantly decreased. The nanoparticles at the zein to lecithin mass ratio of 5:1 had the largest particle size (263 nm), indicating that zein and lecithin formed composite colloidal nanoparticles, which might aggregate due to the enhanced interaction at a higher proportion of lecithin. Continuing to increase lecithin concentration, the zein-lecithin nanoparticles possibly formed a reverse micelle-like or a vesicle-like structure with zein in the core, which prevented the formation of nanoparticle aggregates and decreased the size of composite nanoparticles. The presence of lecithin significantly reduced the ζ-potential of zein-lecithin composite colloidal nanoparticles. The interaction between zein and lecithin enhanced the intensity of the fluorescence emission of zein in ethanol-water solution. The secondary structure of zein was also changed by the addition of lecithin. Differential scanning calorimetry thermograms revealed that the thermal stability of zein-lecithin nanoparticles was enhanced with the rise of lecithin level. The composite nanoparticles were relatively stable to elevated ionic strengths. Possible interaction mechanism between zein and lecithin was proposed. These findings would help further understand the theory of the interaction between the alcohol soluble protein and the natural small molecular surfactant. The composite colloidal nanoparticles formed in this study can broaden the application of zein and be suitable for incorporating water-insoluble bioactive components in functional food and beverage products.

show abstract

“…That a lot of small non‐fibrillar protein aggregates are also present at this pH suggests that some fibrils have disintegrated into small aggregates. In a recent study, Mantovani, Fattori, Michelon, and Cunha () observed a significant effect of soybean lecithin addition on whey protein fibril formation. Indeed, the secondary structure of fibrils formed in the presence or absence of soybean lecithin showed no differences or measurable differences, respectively, when increasing the pH from 3.0 to 7.0.…”

Section: Stability Of (Food) Protein Fibrilsmentioning

confidence: 99%

Rational Design of Amyloid‐Like Fibrillary Structures for Tailoring Food Protein Techno‐Functionality and Their Potential Health Implications

Jansens

Rombouts

Grootaert

et al. 2018

Comp Rev Food Sci Food Safe

120

View full text Add to dashboard Cite

To control and enhance protein functionality is a major challenge for food scientists. In this context, research on food protein fibril formation, especially amyloid fibril formation, holds much promise. We here first provide a concise overview of conditions, which affect amyloid formation in food proteins. Particular attention is directed towards amyloid core regions because these sequences promote ordered aggregation. Better understanding of this process will be key to tailor the fibril formation process. Especially seeding, that is, adding preformed protein fibrils to protein solutions to accelerate fibril formation holds promise to tailor aggregation and fibril techno‐functionality. Some studies have already indicated that food protein fibrillation indeed improves their techno‐functionality. However, much more research is necessary to establish whether protein fibrils are useful in complex food systems and whether and to what extent they resist food processing unit operations. In this review the effect of amyloid formation on gelation, interfacial properties, foaming, and emulsification is discussed. Despite their prevalent role as functional structures, amyloids also receive a lot of attention due to their association with protein deposition diseases, prompting us to thoroughly investigate the potential health impact of amyloid‐like aggregates in food. A literature review on the effect of the different stages of the human digestive process on amyloid toxicity leads us to conclude that food‐derived amyloid fibrils (even those with potential pathogenic properties) very likely have minimal impact on human health. Nevertheless, prior to wide‐spread application of the technology, it is highly advisable to further verify the lack of toxicity of food‐derived amyloid fibrils.

show abstract

Formation and pH-stability of whey protein fibrils in the presence of lecithin

Cited by 94 publications

References 42 publications

Interactions between whey protein or polymerized whey protein and soybean lecithin in model system

Interactions between whey protein or polymerized whey protein and soybean lecithin in model system

The Interaction between Zein and Lecithin in Ethanol-Water Solution and Characterization of Zein–Lecithin Composite Colloidal Nanoparticles

Rational Design of Amyloid‐Like Fibrillary Structures for Tailoring Food Protein Techno‐Functionality and Their Potential Health Implications

Contact Info

Product

Resources

About