Effects of inulins with various molecular weights and added concentrations on the structural properties and thermal stability of heat-induced gliadin and glutenin gels

Guo, Zehang; Liu, Min; Xiang, Xuwen; Wang, Zhirong; Yang, Bing; Chen, Xuhui; Chen, Guangjing; Kan, Jianquan

doi:10.1016/j.lwt.2021.111891

Cited by 20 publications

(12 citation statements)

References 39 publications

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“…Likewise, in the study of Guo et al . (2021), the addition of inulin decreased the fluorescence intensity of glutenin, which was explained as the tryptophan group was buried in the protein aggregation process with the participation of inulin. This phenomenon was called a fluorescence ‘masking’ effect.…”

Section: Resultsmentioning

confidence: 95%

“…2, there were more re-embedded groups in the M-YG group than the M group, which could provide a reasonable explanation that the fluorescence intensity of M-YG was still lower than that of M at 90 °C. Likewise, in the study of Guo et al (2021), the addition of inulin decreased the fluorescence intensity of glutenin, which was explained as the tryptophan group was buried in the protein aggregation process with the participation of inulin. This phenomenon was called a fluorescence 'masking' effect.…”

Section: Fluorescence Spectramentioning

confidence: 91%

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Impacts of yeast β‐glucan on thermal aggregation and flavour adsorption capacity of Spanish mackerel myosin

Yin

et al. 2022

Int J of Food Sci Tech

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The effects of yeast β-glucan (YG) on the aggregation and flavour adsorption capacity of Spanish mackerel myosin under two-step heat treatments were investigated. The surface hydrophobicity and active sulfhydryl content of heat-induced myosin was increased by the addition of YG, reaching the maximum values of 81.46 and 17.49 mol per 10 5 g after heating at 90 °C for 10 min. YG incorporation significantly decreased the α-helix content of myosin to the minimum value of 48.27%, whereas the β-sheet was increased. The addition of YG promoted the unfolding of myosin, exposing more hydrophobic bonding sites, thus enhancing the flavour-binding capacity of myosin. Lengthy heating at 90 °C combined with YG addition accelerated the cross-linking and aggregation of myosin, leading to the re-embedding of the exposed hydrophobic groups as much as the reduction of flavour-binding sites. However, YG's unique porous structure could also boost the flavour adsorption ability of myosin containing YG.

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Section: Resultsmentioning

confidence: 95%

Section: Fluorescence Spectramentioning

confidence: 91%

Impacts of yeast β‐glucan on thermal aggregation and flavour adsorption capacity of Spanish mackerel myosin

Yin

et al. 2022

Int J of Food Sci Tech

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“…CRG and Ly formed soluble complexes as a result of electrostatic interactions. It was conducive to the stability of Ly's secondary structure, thereby increasing the degree of stability to heat, and inhibiting the occurrence of aggregation (Guo et al, 2021).…”

Section: Fluorescence Spectra After Heating Of Ly/crg Composite Syste...mentioning

confidence: 99%

Interaction investigation and phase transition of carrageenan/lysozyme complex system

et al. 2022

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Phase transition of lysozyme/carrageenan (Ly/CRG) complex system with different ratios, pH, ionic strength and temperature conditions was explored through ultraviolet-visible spectrophotometer, fluorescence spectrophotometer, fluorescence microscope, Zeta potential. The results showed that the main force between Ly and CRG is electrostatic interaction, and the Ly/CRG composite system has undergone three phase transition states: co-solubilization, gelation and aggregation. At pH = 1-3, the oppositely charged CRG and Ly form complexes based on electrostatic interaction. Whereas at pH = 12, both CRG and Ly are negatively charged and they repel each other electrostatically. The electrostatic shielding effect of salt ions had a greater impact on the formation of Ly/CRG complex. Temperature had a certain degree of influence on the structure and turbidity of the composite system. The interaction between polysaccharides and proteins can have a significant impact on the structure and stability of complex systems and the study of polysaccharide and protein complexes which will help to expand their application in food and medicine.

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“… Tseng, Xiong, and Boatright (2008) reported that inulin with high DP was more capable of improving the thermal stability and gel-forming properties of soy protein isolate than those with low DP by promoting protein-protein interactions and altering the protein aggregation pattern. On the contrary, Guo et al (2021) and Liu et al (2021) found that inulin with higher DP strongly hindered the aggregation of gluten by weakening hydrophobic interactions and disulfide bonds, finally resulting in more fragile and more open network structures as well as a softer gel. Thus, the results of these previous studies on the mechanism by which the DP of inulin affected the formation of protein gel were inconsistent or contradictory, which could not clearly indicate the possible impact of inulin DP on the potato protein gel and the related underlying mechanism.…”

Section: Introductionmentioning

confidence: 99%

Effects of inulin with different polymerization degrees on the structural and gelation properties of potato protein

Chen,

Wang,

Wang

et al. 2024

Food Chemistry: X

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Effects of inulins with various molecular weights and added concentrations on the structural properties and thermal stability of heat-induced gliadin and glutenin gels

Cited by 20 publications

References 39 publications

Impacts of yeast β‐glucan on thermal aggregation and flavour adsorption capacity of Spanish mackerel myosin

Impacts of yeast β‐glucan on thermal aggregation and flavour adsorption capacity of Spanish mackerel myosin

Interaction investigation and phase transition of carrageenan/lysozyme complex system

Effects of inulin with different polymerization degrees on the structural and gelation properties of potato protein

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