Effects of high hydrostatic pressure on secondary structure and emulsifying behavior of sweet potato protein

Khan, Nasir Mehmood; Mu, Taihua; Sun, Hongnan; Zhang, Miao; Chen, Jing-Wang

doi:10.1080/08957959.2015.1005013

Cited by 20 publications

(9 citation statements)

References 24 publications

(28 reference statements)

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“…EAI and ES index (ESI) were reported to be increased by HPP treatments (200 to 600 MPa) for potato protein at pH 6 to 9 (Khan, Mu, Sun, Zhang, & Chen, 2015). The EAI of red kidney bean protein isolate, similar to its ESI increased significantly from 24.2 to 40.4 m 2 /g with increasing pressure from 0.101 to 400 MPa and then decreased to 33.9 m 2 /g with further increase in pressure to 600 MPa whereas its FC and FS decreased with pressure levels (200 to 600 MPa; Ahmed, Al‐Ruwaih, Mulla, & Rahman, 2018).…”

Section: Modification Of Plant Proteins By Various Processing Techniquesmentioning

confidence: 99%

Modification of plant proteins for improved functionality: A review

Akharume

Aluko

Adedeji

2021

Comp Rev Food Sci Food Safe

300

136

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The market trend towards plant‐based protein has seen a significant increase in the last decade. This trend has been projected to continue in the coming years because of the strong factors of sustainability and less environmental impact associated with the production of plant‐based protein compared to animal, aside from other beneficial health claims and changes in consumers' dietary lifestyles. In order to meet market demand, there is a need to have plant‐based protein ingredients that rival or have improved quality and functionality compared to the traditional animal protein ingredients they may replace. In this review article, we present a detailed and concise summary of the functionality challenges of some plant protein ingredients with associated physical, chemical, and biological processing techniques (traditional and emerging technologies) that have been attempted to enhance them. We cataloged the differences between several studies that seek to address the functionality challenges of selected plant‐based protein ingredients without overtly commenting on a general technique that addresses the functionality of all plant‐based protein ingredients. Additionally, we elucidated the chemistry behind some of these processing techniques and how they modify the protein structure for improved functionality. Although, many food industries are shifting away from chemical modification of proteins because of the demand for clean label product and the challenge of toxicity associated with scale‐up of this technique, so physical and biological techniques are widely being adopted to produce a functional ingredient such as texturized vegetable proteins, hydrolyzed vegetable protein, clean label protein concentrates, de‐flavored protein isolates, protein flour, and grits.

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Section: Modification Of Plant Proteins By Various Processing Techniquesmentioning

confidence: 99%

Modification of plant proteins for improved functionality: A review

Akharume

Aluko

Adedeji

2021

Comp Rev Food Sci Food Safe

300

136

View full text Add to dashboard Cite

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“…This behavior is typical of associative weak interactions [19] and has been reported for different protein-based emulsions. [20][21][22][23][24][25] This physical behavior can be attributed to different microscopic factors, such as changes in spatial distribution of disperse particles due to shear forces, alignment of non-spherical droplets, removal of solvent molecules bonded to droplets, and deformation and rupture of flakes. [26] The Herschel-Bulkley model was well fitted to the data (Table 2), leading to R 2 > 97% and AMPE < 11% for all studied conditions.…”

Section: Influence Of the Number Of Homogenization Passesmentioning

confidence: 99%

Emulsifying properties of β-lactoglobulin and Quillaja bark saponin mixtures: Effects of number of homogenization passes, pH, and NaCl concentration

Faria

Oliveira

Minim

et al. 2016

International Journal of Food Properties

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The effects of number of homogenization passes, pH, and NaCl concentration on the formation and stability of oil-in-water emulsions comprising a mixture of a biosurfactant (Quillaja bark saponin) and a globular protein (β-lactoglobulin) were investigated. The emulsions were characterized as to visual appearance, droplet size, droplet surface charge, and rheology. The emulsions obtained by different conditions (4, 6, or 8 passes; pH 7, 8, or 9; and 0, 100, or 200 mmol L −1 of NaCl) were polydisperse, presented relatively small average droplet sizes (z-average < 323 nm) as well as negative droplet charge (between-20 and-79.6 mV) in all evaluated conditions. Regardless of the number of homogenization passes, the emulsions exhibited low apparent viscosity and pseudoplastic behavior with small yield stress. Viscoelastic behavior was also observed, thus the emulsions were characterized as weak gels. Four homogenization passes were enough to obtain small droplets in the evaluated conditions. Droplet size was not significantly affected by NaCl concentration and pH (p > 0.05). On the other hand, the absolute ζ-potential values significantly decreased and increased upon increased NaCl content and pH, respectively. Regardless of the tested conditions, all emulsions had good stability against phase separation and droplet aggregation, since no significant changes in average droplet size were observed throughout storage (p > 0.05). In the presence of NaCl, in which droplet charge significantly decreased, emulsion was also stable. Thus, we can conclude that electrostatic repulsion as well as steric repulsion was responsible for stabilization.

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“…Therefore, the surface hydrophobicity was reduced [ 45 ]. Khan et al [ 46 ] and Li et al [ 24 ] also found that the interaction between proteins and polysaccharides caused changes in protein secondary structure and aggregation, and that hydrophobic amino acids were less exposed to the protein surface in the presence of polysaccharides. However, the mechanical force in the process of stirring and homogenization destroys and disperses the aggregated and denatured proteins, causing the hydrophobic groups to be fully exposed, allowing proteins to quickly undergo the stages of diffusion, adsorption, structural rearrangement, crosslinking, and solidification to form an interfacial film of bubbles or emulsion droplets [ 47 ].…”

Section: Resultsmentioning

confidence: 99%

Effect of Xanthan Gum, Kappa–Carrageenan, and Guar Gum on the Functional Characteristics of Egg White Liquid and Intermolecular Interaction Mechanism

Gong

Shi

Zheng

et al. 2022

Foods

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This study evaluated the effects of three polysaccharides, xanthan gum (XG), kappa-carrageenan (CA), and guar gum (GG), on the foaming and emulsifying properties of egg white liquid (EWL) and explored the intermolecular interactions and aggregation states in the initial polysaccharide–EWL complex. The results showed that the addition of XG and GG significantly improved the foaming stability of EWL on the one hand, from 66% to 78% and 69%, respectively (p < 0.05). On the other hand, the addition of XG and GG significantly improved the foam uniformity and density, and the average foam area decreased from 0.127 to 0.052 and 0.022 mm2, respectively (p < 0.05). The addition of XG and CA significantly improved the emulsification activity index (from 13.32 to 14.58 and 14.36 m2/mg, respectively, p < 0.05) and the emulsion stability index (from 50.89 to 53.62 and 52.18 min, respectively, p < 0.05), as well as the interfacial protein adsorption at the oil–water interface; it also reduced the creaming index. However, GG negatively affected these indicators. Furthermore, the electrostatic and hydrophobic interactions among molecules in EWL due to XG and the electrostatic, hydrogen bonding, and hydrophobic interactions among molecules in EWL due to CA ultimately led to the irregular aggregation of egg white proteins. Hydrophobic interactions and disulfide bonds between molecules in EWL–containing GG formed filamentous aggregations of egg white proteins. This work reveals that molecules in the polysaccharide–egg white complexes aggregate by interaction forces, which in turn have different effects on the foaming and emulsifying properties of egg white proteins.

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Effects of high hydrostatic pressure on secondary structure and emulsifying behavior of sweet potato protein

Cited by 20 publications

References 24 publications

Modification of plant proteins for improved functionality: A review

Modification of plant proteins for improved functionality: A review

Emulsifying properties of β-lactoglobulin and Quillaja bark saponin mixtures: Effects of number of homogenization passes, pH, and NaCl concentration

Effect of Xanthan Gum, Kappa–Carrageenan, and Guar Gum on the Functional Characteristics of Egg White Liquid and Intermolecular Interaction Mechanism

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