Effect of high intensity ultrasound on the structure and physicochemical properties of soy protein isolates produced by different denaturation methods

Zheng, Ting; Li, Xiaohui; Taha, Ahmed; Yue, W.W.; H, Tan; Fatamorgana, Pijiar Beyna; Zhang, Zhuo; Liu, Fengxia; Xu, Xiaoyun; Pan, Siyi; Hu, Hao

doi:10.1016/j.foodhyd.2019.105216

Cited by 98 publications

(63 citation statements)

References 57 publications

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“…The highly repetitive feature of β-sheet and higher content of ordered structure could be closely correlated with the higher stability of DGH soluble aggregates. Zheng et al [ 6 ] and Hu et al [ 5 ] both observed an increased α-helix content and decreased β-sheet content in the HIU treatment of native SPI (80 W/cm 2 ) and commercial SPI (105–138 W/cm 2 ), which was consistent with the present results of CSPI. However, when the isolated β-conglycinin and glycinin were solely subjected to an equivalent ultrasonication (105–110 W/cm 2 ), neither of them showed significant changes in their secondary structures [ 7 ].…”

Section: Resultssupporting

confidence: 91%

“…However, the longer duration of HIU processing would not promote further aggregation but dissociate those newly formed aggregates. Zheng et al [ 6 ] observed that HIU (80 W/cm 2 ) increased the particle size of native SPI aggregates after 10 min while reducing the particle size after 25 min. Similarly, Shanmugam et al [ 22 ] found the soluble whey/casein aggregates and micellar aggregates were formed during the first 30 min of sonication (0.31 and 0.63 W/cm 3 ), but prolonged sonication caused the partial disruption of whey proteins from these aggregates due to the continuous shear.…”

Section: Resultsmentioning

confidence: 99%

“…The sample supernatants in Section 2.6 were diluted to 0.15 mg/mL and measured in 0.1 cm quartz CD cuvettes. The scan rate, response, and bandwidth were set as 50 nm/min, 4 s, and 1.0 nm, respectively [ 6 ]. The recorded spectra were an average of three scans and corrected by subtracting the spectrum of the protein-free buffer.…”

Section: Methodsmentioning

confidence: 99%

“…Besides this, HIU could also induce the dissociation and/or aggregation of protein molecules. Zheng et al [ 6 ] found that HIU could increase the aggregates in native SPI while dissociating the aggregates in alcohol-denatured and heat moisture-denatured SPI.…”

Section: Introductionmentioning

confidence: 99%

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High-Intensity Ultrasound Treatment on Soy Protein after Selectively Proteolyzing Glycinin Component: Physical, Structural, and Aggregation Properties

Xia

Pan

Cheng

et al. 2020

Foods

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In this study, a novel method called selective proteolysis was applied to the glycinin component of soy protein isolate (SPI), and a degraded glycinin hydrolysate (DGH) was obtained. The effects of high-intensity ultrasound (HIU) treatment (20 kHz at 400 W, 0, 5, 20, and 40 min) on the physical, structural, and aggregation properties of DGH were investigated with the aim to reveal the influence of the selectively hydrolyzing glycinin component on the HIU treatment of soy protein. The effects of HIU on DGH and a control SPI (CSPI) were both time-dependent. HIU induced the formation of soluble aggregates in both samples at an early stage, while it dissociated these newly formed aggregates after a longer duration. Selectively hydrolyzing glycinin contributed to the soluble aggregation by exposing the compact protein structure and producing small protein fractions. The larger extent of hydrophobic interactions and disulfide bonds imparted a higher stability to the soluble protein aggregates formed in DGH. As a result, DGH displayed more ordered secondary structures, a higher solubility, and better gelling properties after the HIU treatment, especially at 20 min. The results of this study will be beneficial to the scientific community as well as industrial application.

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Section: Resultssupporting

confidence: 91%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

High-Intensity Ultrasound Treatment on Soy Protein after Selectively Proteolyzing Glycinin Component: Physical, Structural, and Aggregation Properties

Xia

Pan

Cheng

et al. 2020

Foods

Self Cite

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“…Raman spectroscopy is a direct and non-invasive technique which has been used to study the structure of SPI [24,25]. Each spectrum of the sample was collected at 785 nm laser excitation wavelength, 300 mW laser power, four scans, and 60 s exposure time.…”

Section: Raman Spectroscopymentioning

confidence: 99%

A Study of Structural Change during In Vitro Digestion of Heated Soy Protein Isolates

Tian

Teng

Zhang

et al. 2019

Foods

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Use of soy protein isolate (SPI) as the encapsulating material in emulsions is uncommon due to its low solubility and emulsification potential. The aim of this study was to improve these properties of SPI via heat treatment-induced modifications. We modified SPI under various heating conditions and demonstrated the relationship between structure and in vitro digestibility in simulated gastric fluid by means of Sodium Dodecyl Sulphide-Polyacrylamide Gel Electrophoresis (SDS-PAGE) and Raman spectroscopy. It was found that the degree of hydrolysis (DH) of SPI increased and then decreased upon increasing exposure to heat. Different subunits of conglycinin were digested and degraded by pepsin. Heat treatment improved digestion characteristics that would reduce e the unnecessary loss of protein, offering potential for the efficient delivery of nutrients in nanoemulsions. These results could have significant relevance for research groups that are interested in the biological interactions and activity of functional SPI.

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Modification of rheological properties of animal and vegetable proteins treated with high‐intensity ultrasound: A review

et al. 2023

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The rheological properties of proteins play a role important in the fluid flow, pump selection, equipment design, and product development. In addition, it has been observed that the texture and mouthfeel of foods depend on the viscoelastic properties of their ingredients, especially those that show both elastic and viscous behavior, such as proteins. To improve the functional properties, including the rheological ones, proteins have been subjected to some physical treatments, such as ultrasound, which is considered an emerging green technology. Changes in the properties of proteins by high‐intensity ultrasound vary according to the equipment used, power, frequency, and time of sonication, as well as the intrinsic characteristics of the studied proteins. As pretreatment, ultrasound affects the rheological properties of proteins such as viscosity and storage and loss moduli due to the structural modification of its polypeptide chain, as a consequence of the cavitation phenomenon. In this review, we present the main results of the effect of high‐intensity ultrasound on the rheological properties of animal and vegetable proteins subjected to different conditions such as ultrasound device, power, frequency, wave amplitude, and exposure time mainly. In this context, the information from studies of the impact of ultrasound on the rheological properties of proteins from animal and vegetable sources is important to diversify its possible use as a food ingredient.

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Effect of high intensity ultrasound on the structure and physicochemical properties of soy protein isolates produced by different denaturation methods

Cited by 98 publications

References 57 publications

High-Intensity Ultrasound Treatment on Soy Protein after Selectively Proteolyzing Glycinin Component: Physical, Structural, and Aggregation Properties

High-Intensity Ultrasound Treatment on Soy Protein after Selectively Proteolyzing Glycinin Component: Physical, Structural, and Aggregation Properties

A Study of Structural Change during In Vitro Digestion of Heated Soy Protein Isolates

Modification of rheological properties of animal and vegetable proteins treated with high‐intensity ultrasound: A review

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