Gel properties and structural characteristics of soy protein isolate treated with different salt ions before spray drying combined with dynamic high-pressure micro-fluidization

Li, Zheng; He, Mingyu; Zhang, Xuena; Regenstein, Joe M.; Wang, Zhongjiang; Ma, Zhaolei; Kong, Yang; Wu, Changling; Teng, Fei; Li, Yang

doi:10.1016/j.fbp.2020.10.016

Cited by 17 publications

(8 citation statements)

References 51 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Under the same heat treatment conditions (90 °C, 30 min), the gel strength was found to increase significantly when the pressure was low (0–60 Mpa), with the highest gel strength of 16 g.mm; when the pressure was high, the hardness of HT‐HPH‐11 S gels decreased significantly. The protein aggregation increased the 11 S gel hardness due to the high‐pressure homogenization promoting the chemical reaction and aggregation between 11 S moieties 47 …”

Section: Resultsmentioning

confidence: 99%

“…The protein aggregation increased the 11 S gel hardness due to the high-pressure homogenization promoting the chemical reaction and aggregation between 11 S moieties. 47 Rheological properties of 11 S gels Dynamic rheological measurements can be used to determine the ability of proteins to form gels and the kinetics of protein gel reactions. 48 To elucidate the effect of HPH (0-100 MPa) combined with the heating on the rheological properties of 11 S gels, frequency scans were performed on the gels.…”

Section: Gel Strengthmentioning

confidence: 99%

See 1 more Smart Citation

Effect of high‐pressure homogenization on Ca²⁺‐induced gel formation of soybean 11 S globulin

Sun

Wang

et al. 2023

J Sci Food Agric

View full text Add to dashboard Cite

Background High‐pressure homogenization (HPH) is commonly used as a non‐thermal processing technique for soybean and soy protein products, and the preparation of soy protein gel products often requires the synergistic effect of HPH and heat treatment. The dissociative association behavior of 11 S is the key to the protein gel formation state. In this study, therefore, 11 S thermal gels were prepared by high‐pressure homogenization and co‐induction (90 °C, 30 min) (adding Ca2+ to promote gel formation before heat treatment), and the effects of different high‐pressure homogenization pressures (0–100 MPa) and co‐treatment on the dissociative association behavior of 11 S protein, gel properties, and microstructure of 11 S gels were investigated. Results The results showed that HPH at higher pressures led to the breaking of disulfide bonds of aggregates and disrupted non‐covalent interactions in protein aggregates, leading to collisions between protein aggregates and the reduction of large protein aggregates. High‐pressure homogenization treatment at 60 MPa improved the gel properties of 11 S more. The HPH combined with heating changed the binary and tertiary structure of 11 S soy globulin and enhanced the hydrophobic interaction between 11 S molecules, thus improving the gel properties of 11 S. The change in intermolecular forces reflected the positive effect of HPH treatment on the formation of denser and more homogeneous protein gels. Conclusion In conclusion, high‐pressure homogenization combined with heating can improve the properties of 11 S gels by changing the structure of 11 S protein, providing data and theoretical support for soy protein processing and its further applications. © 2022 Society of Chemical Industry.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Gel Strengthmentioning

confidence: 99%

Effect of high‐pressure homogenization on Ca²⁺‐induced gel formation of soybean 11 S globulin

Sun

Wang

et al. 2023

J Sci Food Agric

View full text Add to dashboard Cite

show abstract

“…3(d)), as a result of there being less protein in the SPI/SSPS dispersions. The fluorescence intensity of the SPI dispersions with ions decreased (except Na + ) because the extension of the protein peptide chain exposed the aromatic heterocyclic hydrophobic group of the tryptophan residues within the SPI molecule, presumably forming a domain that can interact with ions 23 . The interaction between SPI and ions caused the Trp of SPI to be masked and the fluorescence intensity to decrease.…”

Section: Resultsmentioning

confidence: 99%

“…The fluorescence intensity of the SPI dispersions with ions decreased (except Na + ) because the extension of the protein peptide chain exposed the aromatic heterocyclic hydrophobic group of the tryptophan residues within the SPI molecule, presumably forming a domain that can interact with ions. 23 The interaction between SPI and ions caused the Trp of SPI to be masked and the fluorescence intensity to decrease. The fluorescence spectra of SPI with ions exhibited quenching and red shift (329-336 nm), indicating that the chromophore in the tertiary structure of the SPI was changed and exposed to a more hydrophilic environment.…”

Section: Fluorescence Spectral Analysismentioning

confidence: 99%

Metal cation‐induced conformational changes of soybean protein isolate/soybean soluble polysaccharide and their effects on high‐internal‐phase emulsion properties

Zhao,

Wang,

et al. 2023

J Sci Food Agric

View full text Add to dashboard Cite

BACKGROUNDMetal ions commonly inevitably appear in food products and have adverse effects on high‐internal‐phase emulsions (HIPEs) foods, but conformational conversion of soybean protein isolate (SPI)/soybean soluble polysaccharide (SSPS) on the interface layer of HIPEs influenced by different metal ions has rarely been reported.RESULTSHere, the conformational conversion of SPI/SSPS induced by Na+, K+, Ca2+, Mg2+ and Fe3+ ions and its effects on HIPEs were investigated. After adding the ions to SPI and SPI/SSPS dispersions, the particle size and zeta potential results showed different degrees of flocculation; the zeta potential and Fourier transform infrared spectra indicated that SPI and SPI/SSPS changes in structure involve electrostatic interactions and hydrogen bonding. Moreover, Raman spectra showed that the content of β‐sheet of SPI/SSPS HIPEs increased with the addition of Ca2+, Mg2+ and Fe3+, suggesting that SPI molecules at the interface formed a more orderly structure. The ultraviolet and fluorescence results showed that the hydrophobic environment of tryptophan and tyrosine residues inside protein molecules played a vital role in the emulsifying stability of SPI.CONCLUSIONThese findings suggested that the SPI/SSPS complexes for food applications were not susceptible to ions, thus ensuring complex stability, showing potential for commercial application in the production of emulsions. © 2023 Society of Chemical Industry.

show abstract

“…In addition, when a stronger gel is formed, it can more effectively trap and retain water during centrifugation, resulting in an increase in WHC [27]. However, when the homogeneous pressure is high, SPI forms partially insoluble aggregates, and the particle size and functional properties of the insoluble components are different, so SPI mostly forms irregular aggregates, resulting in uneven gel network structure, and the increase of aggregation and precipitation reduces WHC [28].…”

Section: Effect Of Different Homogeneous Pressure Treatments On the W...mentioning

confidence: 99%

Effect of High-Pressure Homogenization on the Properties and Structure of Cold-Induced Chiba Tofu Gel in Soy Protein Isolate

Zheng,

Regenstein,

Wang

2024

Gels

Self Cite

View full text Add to dashboard Cite

In the actual production process of soy protein isolate (SPI), most of the homogeneous operating pressure is controlled below 20 MPa due to the consideration of production safety and the limitation of the pressure control capability of homogeneous equipment. In order to improve the functional properties of SPI and adapt it to actual production, the effects of different homogeneous pressures (4, 8, 10, 12, and 14 MPa) on the structure and gel properties of SPI were studied from the perspective of production control. Compared to the control group, the modified SPI improved the hardness, springiness, cohesiveness, chewiness, and water holding capacity (WHC) of the protein gel (p < 0.05). Rheological analysis shows that both G′ and G″ increase with increasing frequency, reaching a maximum at 12 MPa. The gel intermolecular force results show that the disulfide bond, hydrophobic interaction, and non-disulfide bond are important molecular forces for gel formation. The particle size distribution uniformity of modified SPI was high, and scanning electron microscopy (SEM) analysis showed that the protein gel with a continuous uniform and dense network structure could be formed by high-pressure homogeneous modification. Overall, high-pressure homogenization technology has the potential to improve SPI gel structure and WHC, and 12 MPa modified SPI gel has the most significant effect.

show abstract

Gel properties and structural characteristics of soy protein isolate treated with different salt ions before spray drying combined with dynamic high-pressure micro-fluidization

Cited by 17 publications

References 51 publications

Effect of high‐pressure homogenization on Ca²⁺‐induced gel formation of soybean 11 S globulin

Effect of high‐pressure homogenization on Ca²⁺‐induced gel formation of soybean 11 S globulin

Metal cation‐induced conformational changes of soybean protein isolate/soybean soluble polysaccharide and their effects on high‐internal‐phase emulsion properties

Effect of High-Pressure Homogenization on the Properties and Structure of Cold-Induced Chiba Tofu Gel in Soy Protein Isolate

Contact Info

Product

Resources

About

Gel properties and structural characteristics of soy protein isolate treated with different salt ions before spray drying combined with dynamic high-pressure micro-fluidization

Cited by 17 publications

References 51 publications

Effect of high‐pressure homogenization on Ca2+‐induced gel formation of soybean 11 S globulin

Effect of high‐pressure homogenization on Ca2+‐induced gel formation of soybean 11 S globulin

Metal cation‐induced conformational changes of soybean protein isolate/soybean soluble polysaccharide and their effects on high‐internal‐phase emulsion properties

Effect of High-Pressure Homogenization on the Properties and Structure of Cold-Induced Chiba Tofu Gel in Soy Protein Isolate

Contact Info

Product

Resources

About

Effect of high‐pressure homogenization on Ca²⁺‐induced gel formation of soybean 11 S globulin

Effect of high‐pressure homogenization on Ca²⁺‐induced gel formation of soybean 11 S globulin