The Impact of High-Pressure Processing on the Structure and Sensory Properties of Egg White-Whey Protein Mixture at Acidic Conditions

Zhang, Zhong; Liu, Ying; Lee, Michelle C.; Ravanfar, Raheleh; Qiu, Shuang

doi:10.1007/s11947-019-02397-6

Cited by 18 publications

(9 citation statements)

References 54 publications

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“…Protein denaturation, and to a larger extent, protein structural change, is usually assessed by measuring the turbidity or optical density (OD) at 595 nm [ 36 ]. More specifically, an increase in OD generally correlated to an increase in the formation of protein aggregates [ 37 ], as previously demonstrated for pressure-treated marine [ 38 ], milk [ 39 ], egg [ 40 ], and soy [ 41 ] proteins, as well as mixed protein systems [ 42 ]. Consequently, the increase in turbidity observed in pressure-treated mealworm protein solutions at 345 MPa could indicate the formation of protein aggregates ( Figure 2 ).…”

Section: Discussionsupporting

confidence: 55%

Effect of High Hydrostatic Pressure Intensity on Structural Modifications in Mealworm (Tenebrio molitor) Proteins

Boukil

Marciniak

Mezdour

et al. 2022

Foods

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Processing edible insects into protein extracts may improve consumer acceptability. However, a better understanding of the effects of food processing on the proteins is needed to facilitate their incorporation into food matrices. In this study, soluble proteins from Tenebrio molitor (10% w/v) were pressurized using high hydrostatic pressure (HHP) at 70–600 MPa for 5 min and compared to a non-pressurized control (0.1 MPa). Protein structural modifications were evaluated using turbidity measurement, particle-size distribution, intrinsic fluorescence, surface hydrophobicity, gel electrophoresis coupled with mass spectrometry, and transmission electron microscopy (TEM). The observed decrease in fluorescence intensity, shift in the maximum emission wavelength, and increase in surface hydrophobicity reflected the unfolding of mealworm proteins. The formation of large protein aggregates consisting mainly of hexamerin 2 and ⍺-amylase were confirmed by protein profiles on gel electrophoresis, dynamic light scattering, and TEM analysis. The typical aggregate shape and network observed by TEM after pressurization indicated the potential involvement of myosin and actin in aggregate formation, and these were detected by mass spectrometry. For the first time, the identification of mealworm proteins involved in protein aggregation phenomena under HHP was documented. This work is the first step in understanding the mealworm protein–protein interactions necessary for the development of innovative insect-based ingredients in food formulations.

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Section: Discussionsupporting

confidence: 55%

Effect of High Hydrostatic Pressure Intensity on Structural Modifications in Mealworm (Tenebrio molitor) Proteins

Boukil

Marciniak

Mezdour

et al. 2022

Foods

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“…Importantly, this unique sensation could be triggered by a large variety of natural foods, including red wines (Watrelot, Heymann, & Waterhouse, 2020), green tea (Zhuang et al., 2020), coffee (Barbosa, Scholz, Kitzberger, & Benassi, 2019; Hu et al., 2020), soybean (Ueno, Kawaguchi, Oshikiri, Liu, & Shimada, 2019), various berries (Ciesarová et al., 2020; Kelanne et al., 2019), and so on. From a molecular perspective, the major astringent compounds in natural foods could be classified into phenols, proteins, multivalent metallic salts, organic and mineral acids, and dehydrating agents (such as acetone, glycerin, and ethanol) (Bajec & Pickering, 2008; Joslyn & Goldstein, 1964; Zhang et al., 2020). Different groups of astringent compounds might have diverse bases of astringency mechanisms (Joslyn & Goldstein, 1964), which may be related to the chemical structure of astringents.…”

Section: Introductionmentioning

confidence: 99%

An overview of the perception and mitigation of astringency associated with phenolic compounds

Huang

2020

Comp Rev Food Sci Food Safe

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Astringency, as a kind of puckering, drying, or rough sensation, is widely perceived from natural foods, especially plants rich in phenolic compounds. Although the interaction and precipitation of salivary proteins by phenolic compounds was often believed as the major mechanism of astringency, a definitive theory about astringency is still lacking due to the complex oral sensations. The interaction with oral epithelial cells and the activation of trigeminal chemoreceptors and mechanoreceptors also shed light on some of the phenolic astringency mechanisms, which complement the insufficient mechanism of interaction with salivary proteins. Since phenolic compounds with different types and structures show different astringency thresholds in a certain regularity, there might be some relationships between the phenolic structures and perceived astringency. On the other hand, novel approaches to reducing the unfavorable perception of phenolic astringency have been increasingly emerging; however, the according summary is still sparse. Therefore, this review aims to: (a) illustrate the possible mechanisms of astringency elicited by phenolic compounds, (b) reveal the possible relationships between phenolic structures and perception of astringency, and (c) summarize the emerging mitigation approaches to astringency triggered by phenolic compounds. This comprehensive review would be of great value to both the understanding of phenolic astringency and the finding of appropriate mitigation approaches to phenolic astringency in future research.

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“…2 , different peaks were observed in the regions of around 661, 1074, 1154, 1240, 1315, 1399, 1450, 1537, 1656, 2782, 2927, 2966, 3076 and 3297 cm-1. The band at 1654 cm-1 is related to the α-helix structure of the protein sample [ 33 ]. After HHP treatment in all samples, especially treatment at 600 MPa, the band's intensity increased which indicate the secondary structure of protein and also the interaction of WPC-guar gum have changed [ 33 ].…”

Section: Resultsmentioning

confidence: 99%

The effect of high hydrostatic pressure on the structure of whey proteins-guar gum mixture

Mirarab Razi,

Mohebbi,

Mirzababaee

et al. 2024

Heliyon

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The Impact of High-Pressure Processing on the Structure and Sensory Properties of Egg White-Whey Protein Mixture at Acidic Conditions

Cited by 18 publications

References 54 publications

Effect of High Hydrostatic Pressure Intensity on Structural Modifications in Mealworm (Tenebrio molitor) Proteins

Effect of High Hydrostatic Pressure Intensity on Structural Modifications in Mealworm (Tenebrio molitor) Proteins

An overview of the perception and mitigation of astringency associated with phenolic compounds

The effect of high hydrostatic pressure on the structure of whey proteins-guar gum mixture

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