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  • Yin, Qi  (3)
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  • 1
    Online Resource
    Online Resource
    The preparation of soy glycinin/sugar beet pectin complex network gels catalyzed by laccase under weakly acidic conditions
    Wiley ; 2023
    In:  Journal of the Science of Food and Agriculture Vol. 103, No. 8 ( 2023-06), p. 4131-4142
    Details
    In: Journal of the Science of Food and Agriculture, Wiley, Vol. 103, No. 8 ( 2023-06), p. 4131-4142
    Abstract: Traditional soy protein gel products such as tofu, formed from calcium sulfate or magnesium chloride, have poor textural properties and water retention capacity. Soy glycinin (SG) is the main component affecting the gelation of soy protein and can be cross‐linked with polysaccharides, such as sugar beet pectin (SBP), and can be modified by changing system factors (e.g., pH) to improve the gel's properties. Soy glycinin/sugar beet pectin (SG/SBP) complex double network gels were prepared under weakly acidic conditions using laccase cross‐linking and heat treatment. The structural changes in SG and the properties of complex gels were investigated. RESULTS Soy glycinin exposed more hydrophobic groups and free sulfhydryl groups at pH 5.0. Under the action of laccase cross‐linking, SBP could promote the unfolding of SG tertiary structures. The SG/SBP complex gels contained 46.77% β ‐fold content and had good gelling properties in terms of hardness 290.86 g, adhesiveness 26.87, and springiness 96.70 mm at pH 5.0. The T 22 relaxation time had the highest peak, and magnetic resonance imaging (MRI) showed that the gel had even water distribution. Scanning electron microscopy (SEM) and confocal scanning laser microscopy (CLSM) indicated that the SG/SBP complex network structure was uniform, and the pore walls were thicker and contained filamentous structures. CONCLUSION Soy glycinin/ sugar beet pectin complex network gels have good water‐holding, rheological, and textural properties at pH 5.0. The properties of soy protein gels can be improved by binding to polysaccharides, with laccase cross‐linked, and adjusting the pH of the solution. © 2022 Society of Chemical Industry.
    Type of Medium: Online Resource
    ISSN: 0022-5142 , 1097-0010
    URL: Issue
    URL: Article
    DOI: 10.1002/jsfa.v103.8
    DOI: 10.1002/jsfa.12408
    Language: English
    Publisher: Wiley
    Publication Date: 2023
    detail.hit.zdb_id: 2001807-1
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  • 2
    Online Resource
    Online Resource
    Effect of sodium trimetaphosphate on the physicochemical properties of modified soy protein isolates and its lutein‐loaded emulsion
    Wiley ; 2023
    In:  Journal of Food Science Vol. 88, No. 2 ( 2023-02), p. 744-756
    Details
    In: Journal of Food Science, Wiley, Vol. 88, No. 2 ( 2023-02), p. 744-756
    Abstract: Due to people's pursuit of healthy and green life, soy protein isolate (SPI) is occupying a larger and larger market share. However, the low solubility of SPI affects its development in the field of food and medicine. This paper aimed to investigate the effects of sodium trimetaphosphate (STMP) on the functional properties and structures of phosphorylated SPI and its lutein‐loaded emulsion. After modification by STMP, the phosphorus content of phosphorylated SPI reached 1.2–3.61 mg/g. Infrared spectrum and X‐ray photoelectron spectrum analysis confirmed that PO 4 3− had phosphorylation with –OH in serine of SPI molecule. X‐ray diffraction analysis showed that phosphorylation destroyed the crystal structure of protein molecules. Zeta potential value of phosphorylated SPI decreased significantly. When STMP addition was 100 g/kg, particle size of protein solution decreased to 203 nm, and solubility increased to 73.5%. Furthermore, emulsifying activity and emulsifying stability increased by 0.51 times and 8 times, respectively. At the same protein concentration (1%–3% [w/w] ), lutein‐loaded emulsion prepared by phosphorylated SPI had higher absolute potential and smaller particle size. The phosphorylated protein emulsion at 2% concentration had the best emulsion stability after storage for 17 days. Practical Application Phosphorylation significantly improved the emulsifying properties and solubility of SPI. Phosphorylated SPI significantly improved the stability of lutein‐loaded emulsion. It provides theoretical basis for the application of phosphorylated SPI as emulsifier in delivery system and broadens the development of lutein in food and medicine field.
    Type of Medium: Online Resource
    ISSN: 0022-1147 , 1750-3841
    URL: Issue
    URL: Article
    DOI: 10.1111/jfds.v88.2
    DOI: 10.1111/1750-3841.16446
    Language: English
    Publisher: Wiley
    Publication Date: 2023
    detail.hit.zdb_id: 2006705-7
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  • 3
    Online Resource
    Online Resource
    Preparation of high complex concentration emulsion stabilized by soy protein/dextran sulfate composite particles
    Wiley ; 2023
    In:  Journal of the Science of Food and Agriculture Vol. 103, No. 12 ( 2023-09), p. 5904-5915
    Details
    In: Journal of the Science of Food and Agriculture, Wiley, Vol. 103, No. 12 ( 2023-09), p. 5904-5915
    Abstract: Soy protein isolate (SPI) can be used as an emulsifier to stabilize emulsions, though SPI is unstable under low acidic conditions. Stable composite particles of SPI and dextran sulfate (DS) can be formed by the electrostatic interaction at the pH 3.5. Furthermore, the SPI/DS composite particles can be used to prepare a high complex concentration emulsion. The stabilization properties of the high complex concentration emulsion were investigated. RESULTS Compared to uncompounded SPI, the particle size of SPI/DS composite particles was smaller at 1.52 μm, and the absolute value of the potential increased to 19.9 mV when the mass ratio of SPI to DS was 1:1 and the pH was 3.5. With the DS ratio increased, the solubility of the composite particles increased to 14.44 times of the untreated protein at pH 3.5, while the surface hydrophobicity decreased. Electrostatic interactions and hydrogen bonds were the main forces between SPI and DS, and DS was electrostatically adsorbed on the surface of SPI. The emulsion stability significantly enhanced with the increase of complex concentration (38.88 times higher than at 1% concentration), the emulsion average droplet size was the lowest (9.64 μm), and the absolute value of potential was the highest (46.67 mV) when the mass ratio of SPI to DS was 1:1 and the complex concentration of 8%. The stability of the emulsion against freezing was improved. CONCLUSION The SPI/DS complex has high solubility and stability under low acidic conditions, and the emulsion of the SPI/DS complex has good stability. © 2023 Society of Chemical Industry.
    Type of Medium: Online Resource
    ISSN: 0022-5142 , 1097-0010
    URL: Issue
    URL: Article
    DOI: 10.1002/jsfa.v103.12
    DOI: 10.1002/jsfa.12663
    Language: English
    Publisher: Wiley
    Publication Date: 2023
    detail.hit.zdb_id: 2001807-1
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