Research progress and the application of near-infrared spectroscopy in protein structure and molecular interaction analysis

Chen, Yu; Liang, Dong; Cui, Yinan; Zhao, Bing; Dong, Qin; Wu, Aoli; Li, Lian; Zang, Hengchang

doi:10.1016/j.vibspec.2022.103390

Cited by 11 publications

(5 citation statements)

References 160 publications

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“…Compared with HG gels, the addition of TGase may serve to further covalently cross-link MGSI molecules internally or intermolecularly, forming gel particles that are aggregated and have a thicker interfacial protein layer, making interaction with small-molecule oil droplets more difficult and therefore reducing emulsification. This is consistent with the study conducted by FLANAGAN et al [ 20 ]. Compared with TG gels, MTG gels have improved emulsification activity and reduced emulsion stability.…”

Section: Results and Analysissupporting

confidence: 94%

“…FTIR spectroscopy was used to analyze and characterize the molecular structure of proteins by comparing the differences in absorbance of different groups in their corresponding optical absorption regions and is at present widely used to verify protein–polysaccharide interactions and to assess structural changes in glycosylated proteins. The characteristic absorption bands of the IR scan include the amide I band (1600–1700 cm −1 , H-O-H bending, and C=O stretching vibrations), the amide II band (1530–1550 cm −1 , N-H bending), and the amide III band (1260–1330 cm −1 , C-O and C-O) [ 20 ]. The FTIR spectra of MGSI and the three protein gel particles (HG, TG, and MTG gels) are presented in Figure 2 .…”

Section: Results and Analysismentioning

confidence: 99%

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The Effect of Different Induction Methods on the Structure and Physicochemical Properties of Glycosylated Soybean Isolate Gels

Sun

Zhang

et al. 2022

Foods

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Soybean protein isolate (SPI), as a full-valued protein, is rich in nutrients, such as amino acids. However, the isolated structure of soybeans makes it difficult to react and thus prepare good gels. In order to further improve the properties of SPIs and to prepare plant-based gels with good performance, this experiment was conducted to prepare maltodextrin glycosylated soybean isolate (MGSI) by the glycosylation of SPI and maltodextrin (MD), and the gels were prepared by thermal induction, transglutaminase (TGase) induction, and TG-MgCl2 co-induction of this glycosylated protein to investigate the effects of different induction methods on the structure and properties of the gels produced by MGSIs. Moreover, the effects of different induction methods on the structure and properties of the gels produced by MGSI were investigated. SDS-PAGE protein electrophoresis, FTIR spectroscopy, and endogenous fluorescence spectroscopy revealed that all three inductions result in the covalent bond cross-linking of MGSI during the gel formation process. Compared with thermal induction, the TGase-induced MGSI secondary structure had a higher content of β-folded structures, increased fluorescence intensity of tertiary structures, and produced a red shift. The gel induced by TGase in collaboration with MgCl2 contains a more β-folded structure and irregular curl and increases the β-turned angle and α-helix content further, the endogenous fluorescence λmax is significantly red-shifted, and the fluorescence intensity increases, demonstrating that the tertiary structure of MGSI unfolds the most, forming multilayered gels with the tightest structures. The three gels were analyzed by rheology and SEM, showing that the TGase-MgCl2 synergistically induced gel had the highest energy-storage modulus G’, viscoelasticity, and water-holding capacity, as well as the densest gel structure. In conclusion, the combined treatment of enzyme and MgCl2 might be an effective way of improving the structure and gel properties of SPI. This study helps to promote the high-value utilization of SPI and the development of plant protein gels.

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Section: Results and Analysissupporting

confidence: 94%

Section: Results and Analysismentioning

confidence: 99%

The Effect of Different Induction Methods on the Structure and Physicochemical Properties of Glycosylated Soybean Isolate Gels

Sun

Zhang

et al. 2022

Foods

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“…Proteins are biological macromolecules with specific structures formed by connecting amino acids through skin bonds. The main active groups are peptide bonds, aromatic amino acid residues, and disulfide bonds in the skin chain skeleton ( 17 ). The changes in the secondary structure content of protein in egg yolk during storage are shown in Figure 1 .…”

Section: Resultsmentioning

confidence: 99%

Supplemental methionine selenium effects on egg yolk physicochemical, functional, and protein structure during storage

Chen

Liu

2023

Front. Nutr.

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To clarify the effect of the addition of methionine selenium on the physicochemical, functional, and protein structural properties of egg yolk during storage. We analyzed the changes in the main indicators of egg yolks stored at 4°C and 25°C for 28 days. The results showed that the increase in water content and pH, and the decrease in absolute zeta potential and apparent viscosity of the selenium-rich egg yolks (Se-group) during storage were smaller than those of the control group egg yolks (C-group). In addition, the antioxidant capacity and emulsifying ability of the Se-group during storage were better than those of the C-group. Simultaneously, the hardness and chewiness of the Se-group gel during storage were lower than those of the C-group. The protein structure results showed that selenium rich treatment did not affect the secondary structure of egg yolk protein during storage but could improve the fluorescence intensity of the egg yolk protein. Therefore, the addition of methionine selenium can reduce the degree of deterioration in the physicochemical properties of egg yolk during storage and extend its shelf life.

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“…Physical, chemical and mechanical effects due to cavitation are the main mechanisms leading to conformational changes in proteins, including high temperature and pressure, microjet, shear forces, microturbulence, formation of radicals and peroxides (Wen et al, 2018). Proteins can be classified into primary, secondary, tertiary and quaternary structures (Yu et al, 2022;Huang et al, 2023). The primary structure refers to the linear arrangement of amino acids.…”

Section: Effects Of Ultrasound On Protein Structurementioning

confidence: 99%

Research progress and latest application of ultrasonic treatment on protein extraction and modification

Zhang,

Ji,

Liang

et al. 2024

Int J of Food Sci Tech

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SummaryThe advancement of the modern food industry has prompted a shift away from traditional protein extraction methods due to their inherent limitations. As a result, there is a growing interest in exploring alternative methods for protein extraction and modification such as ultrasonic (US) treatment. This shift towards more sustainable and efficient protein extraction methods is a key research focus in obtaining safe proteins in an environmentally friendly manner. Furthermore, enhancing the functional properties of proteins through modification can expand their application. This paper reviews recent research progress and applications of US treatment on protein extraction and modification as well as the impact on protein structure and functional properties. In addition, the latest applications of ultrasound‐modified‐proteins, including nano‐proteins, 3D printing and interactions between proteins and other food components, are reviewed. This review may provide some inspiration for the potential application of US technologies in food fields.

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Research progress and the application of near-infrared spectroscopy in protein structure and molecular interaction analysis

Cited by 11 publications

References 160 publications

The Effect of Different Induction Methods on the Structure and Physicochemical Properties of Glycosylated Soybean Isolate Gels

The Effect of Different Induction Methods on the Structure and Physicochemical Properties of Glycosylated Soybean Isolate Gels

Supplemental methionine selenium effects on egg yolk physicochemical, functional, and protein structure during storage

Research progress and latest application of ultrasonic treatment on protein extraction and modification

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