Microfluidization as a potential technique to modify surface properties of soy protein isolate

Shen, Lan; Tang, Chuan-He

doi:10.1016/j.foodres.2012.03.006

Cited by 234 publications

(95 citation statements)

References 38 publications

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“…It indicated that DHPM treatment could make molecule unfolding and expose more hydrophobic domains to the surface. Previous literatures also showed the higher H 0 values of proteins treated by DHPM (Bouaouina et al, ; Hu, Zhao, Sun, Zhao, & Ren, ; Shen & Tang, ).…”

Section: Resultsmentioning

confidence: 67%

“…With short executing time, DHPM treatment did not break down fish gelatin into smaller entities. Similarly, DHPM also could not cause subunit dissociation of peanut protein isolate (Hu et al, ), whey protein (Bouaouina et al, ), soy protein isolate (Shen & Tang, ), and trypsin (Liu et al, ). The unchanged molecular weight distribution of fish gelatin could explain why there was no variance of gel strength among different pressure treated fish gelatin.…”

Section: Resultsmentioning

confidence: 99%

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Influence of dynamic high pressure microfluidization on functional properties and structure of gelatin from bighead carp (Hypophthalmichthys nobilis ) scale

Sha

et al. 2018

J Food Process Preserv

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Dynamic high pressure microfluidization (DHPM) was applied to treat fish gelatin from bighead carp (Hypophthalmichthys nobilis) scale. The effects of various pressures from 40 to 160 MPa on the functional properties and structural characteristics of fish gelatin were evaluated. The results showed that DHPM significantly improved the emulsifying and foaming properties, as well as the in vitro pepsin digestibility. Surface hydrophobicity of treated fish gelatin was considered to be highly correlated to emulsifying activity with R2 of .99933. DHPM could not change gel strength and molecular weight distribution of fish gelatin, but decreased its melting temperature with the increased pressures. Micro‐structural analysis showed that DHPM endowed fish gelatin with polyporous, rough but uncracked microstructure. Practical applications In spite of possessing relatively low melting temperature, fish gelatin is a suitable replacement for mammalian gelatin in low‐temperature stored foods including milk and yogurt. At this time, surface‐active properties including foaming and emulsifying properties are generally the most important factor for ensuring food quality. However, fish gelatin shows relatively weaker surface‐active properties, especially emulsifying/stabilizing function. Our results show DHPM is a physical technology to enhance the surface‐active properties of fish gelatin. DHPM will be promising to promote fish gelatin for its applications in the food industry.

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Section: Resultsmentioning

confidence: 67%

Section: Resultsmentioning

confidence: 99%

Influence of dynamic high pressure microfluidization on functional properties and structure of gelatin from bighead carp (Hypophthalmichthys nobilis ) scale

Sha

et al. 2018

J Food Process Preserv

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“…Because Trp residues of a protein are excited at 280 nm, the changes in the tertiary structure of the protein can be determined from the fluctuations of the fluorescence. [39,40] In plant protein, two aromatic amino acid residues, tryptophan (Trp) and tyrosine (Tyr), make the major contribution to the ultraviolet fluorescence of the protein. As the energy transfer from the tyrosine residues to the tryptophan residues leads to quenching of the fluorescence of the tyrosine residues and enhancement of the fluorescence of the tryptophan residues, it is generally accepted that the protein fluorescence results mainly from the fluorescence of Trp residues, whose peak position is between 325 and 350 nm.…”

Section: Fluorescence Spectrummentioning

confidence: 99%

Structural and functional properties of Maillard reaction products of protein isolate (mung bean,Vigna radiate(L.)) with dextran

Zhou

Zhang

et al. 2017

International Journal of Food Properties

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The objective of this study was to determine the functional and structural properties of Maillard reaction products of mung bean [Vigna radiate (L.)] protein isolate with dextran obtained under the temperature of 80°C or 90°C with different times (0, 1, 2, 3, 4, 5, and 6 h). The mung bean protein isolate-dextran conjugate had better solubility, emulsifying activity, and emulsifying stability than mung bean protein isolate; however, the protein aggregation decreased the solubility, surface hydrophobicity, emulsifying activity, and emulsifying stability of mung bean protein isolate-dextran conjugate. In general, these functional properties of mung bean protein isolate-dextran conjugate obtained at 80°C with lower degree of glycosylation and browning degree were better than mung bean protein isolatedextran conjugate obtained at 90°C. Both vicilin (8S) and legumin type (11S) globulins both participated in the graft reaction, the subunit with a molecular weight of 21 kDa that contributed to 11S globulin might be the most vulnerable to dextran followed by the 60, 32, and 26 kDa subunits. Maillard reaction between mung bean protein isolate and dextran led to a decreased fluorescence intensity and a bathochromic shift. The fluorescence intensity of mung bean protein isolate-dextran conjugate generally decreased, and λ max of mung bean protein isolate-dextran conjugate first increased and then decreased. The grafted mung bean protein isolates had lower α-helix content but higher β-sheet content. As the Maillard reaction between mung bean protein isolate and dextran proceeded, the α-helix contents of the mung bean protein isolate-dextran conjugates were significantly increased and then decreased, and the β-sheet content generally decreased and then increased. Excessive grafted dextran and more protein aggregation was observed in mung bean protein isolate-dextran conjugate obtained at 90°C, which induced structural changes that might have impaired the functions. Our findings suggest that conjugation of mung bean protein isolate with dextran through the Maillard reaction is an effective way of improving the functional properties of mung bean protein isolate for its application in the food industry. ARTICLE HISTORY

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“…As expected, the heat treatment above the thermo‐denaturation temperature of albumins (approximately 58 °C according to Djoullah et al. ()) caused the unfolding and denaturation of protein molecules, which associated to form aggregates, through mainly intermolecular attractive hydrophobic interaction (Amagliani & Schmitt, ; Shen & Tang, ).…”

Section: Resultsmentioning

confidence: 59%

“…At pH 7, surface hydrophobicity of AA increased after microfluidization and with the applied pressure. Increased hydrophobicity during microfluidization has already been observed at neutral pH for heat‐treated soy globulins homogenized at 120 MPa (Shen & Tang, ) and for whey protein aggregates treated at >120 MPa pressures (Liu et al., ). Recent works in our group (Oliete et al., , ) indicated an opposite effect for pea‐Glob aggregates showing the decrease in surface hydrophobicity of the protein particles after microfluidization.…”

Section: Discussionmentioning

confidence: 88%

The Effect of High‐Pressure Microfluidization Treatment on the Foaming Properties of Pea Albumin Aggregates

Djemaoune

Cases

Saurel

2019

Journal of Food Science

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The effect of dynamic high‐pressure treatment, also named microfluidization, on the surface properties of thermal pea albumin aggregates (AA) and their foaming ability was investigated at pH 3, 5, and 7. The solubility of albumin particles was not affected by the increase in microfluidization pressure from 70 to 130 MPa. Particle charge depended only on the pH, whereas protein surface hydrophobicity was stable at pH 5, decreased at pH 3, but increased at pH 7 after microfluidization treatment and with the applied pressure. Surface tension of AA measured at air/water interface was favorably affected by the microfluidization treatment at each pH preferentially due to size reduction and increased flexibility of protein particles. The foaming capacity and stability of AA depended on the pH conditions and the microfluidization treatment. The high‐pressure treatment had little influence in foaming properties at acidic pHs, probably related to a more compact form of AA at these pHs. At neutral pH, the foaming properties of pea AA were strongly influenced by their surface properties and size associated with significant modifications in AA structure with microfluidization. Changes in albumin aggregate characteristics with pH and microfluidization pressure are also expected to modulate other techno‐functional properties, such as emulsifying property. Practical Application Albumins are known for their interesting nutritional values because they are rich in essential amino acids. This fraction is not currently marketed as a protein isolate for human consumption, but can be considered as a potential new vegetable protein ingredient. This document demonstrated that heat treatment or dynamic high‐pressure technology can control the foaming properties of this protein for possible use in expanded foods.

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Microfluidization as a potential technique to modify surface properties of soy protein isolate

Cited by 234 publications

References 38 publications

Influence of dynamic high pressure microfluidization on functional properties and structure of gelatin from bighead carp (Hypophthalmichthys nobilis ) scale

Influence of dynamic high pressure microfluidization on functional properties and structure of gelatin from bighead carp (Hypophthalmichthys nobilis ) scale

Structural and functional properties of Maillard reaction products of protein isolate (mung bean,Vigna radiate(L.)) with dextran

The Effect of High‐Pressure Microfluidization Treatment on the Foaming Properties of Pea Albumin Aggregates

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