High-temperature glycosylation modifies the molecular structure of ovalbumin to improve the freeze-thaw stability of its high internal phase emulsion

Lu, Fei; Ma, Yufeng; Zang, Jingnan; Qing, Mingmin; Ma, Zihong; Chi, Yujie; Chi, Yuan

doi:10.1016/j.ijbiomac.2023.123560

Cited by 25 publications

(3 citation statements)

References 54 publications

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“…As a solvent of wet‐ heating method, water inhibits the glycosylation reaction from going forward in some extent because it is also the product of Maillard primary stage. Additionally, high temperatures under wet‐heating condition and electrostatic charge interaction on molecular surface lead to aggregation and generation of complex Maillard end products (Lu et al., 2024). Therefore, the control of wet heating glycosylation reactions and the complexity of the products are issues that still need to be addressed.…”

Section: Preparation and Quantification Of Glycosylation Productsmentioning

confidence: 99%

Effect of glycosylation modification on structure and properties of soy protein isolate: A review

Chen,

Zhang,

Chen

et al. 2024

Journal of Food Science

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Soybean protein isolate (SPI) is a highly functional protein source used in various food applications, such as emulsion, gelatin, and food packaging. However, its commercial application may be limited due to its poor mechanical properties, barrier properties, and high water sensitivity. Studies have shown that modifying SPI through glycosylation can enhance its functional properties and biological activities, resulting in better application performance. This paper reviews the recent studies on glycosylation modification of SPI, including its quantification method, structural improvements, and enhancement of its functional properties, such as solubility, gelation, emulsifying, and foaming. The review also discusses how glycosylation affects the bioactivity of SPI, such as its antioxidant and antibacterial activity. This review aims to provide a reference for further research on glycosylation modification and lay a foundation for applying SPI in various fields.

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Section: Preparation and Quantification Of Glycosylation Productsmentioning

confidence: 99%

Effect of glycosylation modification on structure and properties of soy protein isolate: A review

Chen,

Zhang,

Chen

et al. 2024

Journal of Food Science

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“…For example, net charges, surface hydrophobicity, and emulsifying activity were significantly improved after coconut protein isolate glycosylation with pectin [8]. Compared with untreated ovalbumins, glycation with fructose decreased the particle sizes and net charges and increased surface hydrophobicity of the ovalbumins, and, therefore, conjugate-stabilized HIPE exhibited smaller droplet sizes and better freeze-thaw stability [6]. In addition, many studies proved a correlation between protein interfacial properties and emulsification activity, i.e., the higher the interfacial activity, the better the emulsification activity.…”

Section: Introductionmentioning

confidence: 99%

“…Especially, multiple investigations have demonstrated that proteinpolysaccharide conjugates exhibited enhanced interfacial adsorption and accumulation and the formation of viscoelastic interfacial layers, remarkably improving the emulsifying capability [3]. For instance, glycated proteins, such as soy protein isolates [4], soy glycinin [5], ovalbumin [6], and pecan protein [7], showed improved emulsifying efficiency for stabilizing HIPE with thermal and antioxidant stability or coalescence stability against storage. However, the stabilization mechanism of HIPE by glycated proteins with enhanced emulsification activity was still unknown.…”

Section: Introductionmentioning

confidence: 99%

Glycation Improved the Interfacial Adsorption and Emulsifying Performance of β-Conglycinin to Stabilize the High Internal Phase Emulsions

Zhang

Tian

Pan

et al. 2023

Foods

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This study investigated the interfacial adsorption and emulsifying performance of glycated β-conglycinin (7S) with D-galactose (Gal) at various times. Results indicated that glycation increased the particle sizes and zeta potentials of glycated 7S by inducing subunit dissociation. Glycation destroyed the tertiary structures and transformed secondary structures from an ordered one to a disordered one, leading to the more flexible structures of glycated 7S compared with untreated 7S. All these results affected the structural unfolding and rearrangement of glycated 7S at the oil/water interface. Therefore, glycated 7S improved interfacial adsorption and formed an interfacial viscoelasticity layer, increasing emulsifying performance to stabilize high internal phase emulsions (HIPE) with self-supportive structures. Furthermore, the solid gel-like network of HIPE stabilized by glycated 7S led to emulsification stability. This result provided new ideas to improve the functional properties of plant proteins by changing the interfacial structure.

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Freeze–thaw stability of high‐internal‐phase emulsion stabilized by chickpea protein microgel particles and its application in surimi

Xu,

Fan,

2024

J Sci Food Agric

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BACKGROUNDFuture applications of high‐internal‐phase emulsions (HIPEs) are highly regarded, but poor freeze–thaw stability limits their utilization in frozen products. This study aimed to characterize the structure of chickpea protein microgel particles (HCPI) induced by NaCl and to assess its impact on the freeze–thaw stability of HIPEs.RESULTSThe results showed that NaCl induction (0–400 mmol L−1) increased the surface hydrophobicity (175.9–278.9) and interfacial adsorbed protein content (84.9%–91.3%) of HCPI. HIPEs prepared with HCPI induced by high concentration of NaCl exhibited superior flocculation index and centrifugal stability, and their freeze–thaw stability was better than that of natural chickpea protein. The increase in NaCl concentration reduced the droplet aggregation and coalescence index of the freeze–thaw emulsions, diminishing the precipitation of oil from the emulsion. Linear and nonlinear rheology showed that the strengthened gel structure (higher G′ values) restricted water flow and counteracted the damage to the interfacial film by ice crystals at 100–400 mmol L−1 NaCl, thus improving the viscoelasticity of the freeze–thaw emulsions. Finally, the thawing loss of surimi gel with HCPI‐200 HIPE was reduced by 2.04% compared to directly adding oil.CONCLUSIONThis study provided a promising strategy to improve the freeze–thaw stability of HIPEs and reduce the thawing loss of frozen products. © 2024 Society of Chemical Industry.

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High-temperature glycosylation modifies the molecular structure of ovalbumin to improve the freeze-thaw stability of its high internal phase emulsion

Cited by 25 publications

References 54 publications

Effect of glycosylation modification on structure and properties of soy protein isolate: A review

Effect of glycosylation modification on structure and properties of soy protein isolate: A review

Glycation Improved the Interfacial Adsorption and Emulsifying Performance of β-Conglycinin to Stabilize the High Internal Phase Emulsions

Freeze–thaw stability of high‐internal‐phase emulsion stabilized by chickpea protein microgel particles and its application in surimi

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