Effects of acylation and glycation treatments on physicochemical and gelation properties of rapeseed protein isolate

Wang, Zhigao; Zhang, Cheng; Zhang, Tian; Ju, Xingrong; He, Rong

doi:10.1039/c8ra07912a

Cited by 36 publications

(13 citation statements)

References 44 publications

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“…The secondary protein structures were mainly composed of β‐sheet (at 1615–1640 cm −1 and 1689–1698 cm −1 region), β‐turn (at 1660–1688 cm −1 region), α‐helix (1650–1659 cm −1 region), random coil (1641–1649 cm −1 region) (Wang et al., 2018). The proportion of the secondary structure of MOSSP is presented in Table 1.…”

Section: Resultsmentioning

confidence: 99%

Influences of ultrasonic treatment on structure and functional properties of salt‐soluble protein from Moringa oleifera seeds

Tang

Ren

et al. 2021

Int J of Food Sci Tech

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Summary Influences of ultrasonic treatment on structure and functional properties of salt‐soluble protein from Moringa oleifera seeds (MOSSP) were explored. The results indicated that the ultrasonic treatment destroyed spherical structure of MOSSP and transformed the spherical structure into irregular fragments. The content of β‐turn, α‐helix and random coils in MOSSP significantly increased, but with extending the ultrasound time, the content of β‐turn, α‐helix and random coils had no significant change. SDS‐PAGE results showed that sonication could stabilise the primary structure of MOSSP. The surface hydrophobicity and emulsification were significantly reduced, but sonication could improve the solubility and foaming properties of MOSSP within a certain range.

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Section: Resultsmentioning

confidence: 99%

Influences of ultrasonic treatment on structure and functional properties of salt‐soluble protein from Moringa oleifera seeds

Tang

Ren

et al. 2021

Int J of Food Sci Tech

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“…The EAI and ESI reached their maximum values at an SA/SPI mass ratio of 15% with 52.58 m 2 g −1 and 121.84 min respectively. The reason for this change might be attributed to the unfolding of the secondary conformation of the protein during the succinylation treatment; that is, the reduction of the β ‐sheet content and the increase in the random coil content 50 . Meanwhile, an enhancement of protein flexibility affected the protein–lipid interaction and the structural rearrangement of the proteins at the oil–water interface, promoting protein diffusion at the oil–water interface and the formation of interfacial films around the emulsion droplets 27 .…”

Section: Resultsmentioning

confidence: 99%

“…The reason for this change might be attributed to the unfolding of the secondary conformation of the protein during the succinylation treatment; that is, the reduction of the ⊎-sheet content and the increase in the random coil content. 50 Meanwhile, an enhancement of protein flexibility affected the protein-lipid interaction and the structural rearrangement of the proteins at the oil-water interface, promoting protein diffusion at the oil-water interface and the formation of interfacial films around the emulsion droplets. 27 Generally, flexible proteins have better emulsification properties and, conversely, rigid proteins have poor emulsification properties.…”

Section: Interfacial Functional Properties Analysis Emulsifying Prope...mentioning

confidence: 99%

Relationship between flexibility and interfacial functional properties of soy protein isolate: succinylation modification

et al. 2022

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BACKGROUND: In this paper, the effects of different succinic anhydride (SA) additions on the flexibility of soy protein isolate (SPI) were investigated, and changes in protein conformation and interfacial functional properties were measured. The structure-effect relationship between conformation, flexibility, and interfacial functional properties was established.RESULTS: SPI was bound to SA through disulfide bonds, and the zeta potential was reduced. The ⊎-sheet content decreased, the disordered structure increased, and there were changes in tertiary structure and microstructure. The surface hydrophobicity, disulfide bond content, and solution turbidity were reduced to 5063, 1.0967 ∼mol g −1 , and 0.0036 ∼mol g −1 respectively. The best flexibility of SPI (0.3977) and interfacial functional properties were obtained when the mass ratio of SA/SPI was 15%. Correlation analysis showed a highly significant positive correlation (P < 0.01) between flexibility and emulsification and foaming properties, with correlation coefficients of 0.960 and 0.942 for flexibility with emulsifying activity and emulsion stability respectively, and 0.972 and 0.929 for flexibility with foaming capacity and foaming stability respectively. CONCLUSION: The results suggest that succinylation-induced conformational changes of SPI improved its interfacial functional properties by changing its flexibility. These results provide theoretical guidelines for the development and application of highly emulsifiable and stable soy protein products utilizing succinylation.

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“…Therefore, how glycation and glycation parameters would have affected the total solubility was quite significant. In the literature, it was reported that glycation could enhance the solubility of a protein because the pH of the environment during the reaction may lead to structural changes such as disruption of large aggregates, which increase the protein solubility (Wang et al ., 2018). Furthermore, with the addition of reducing sugars in the reaction, a well‐dispersed aqueous phase with a more hydrophilic environment may occur, and this inhibits the aggregation of the proteins, thereby enhancing the interaction with the aqueous phase (Wen et al ., 2020).…”

Section: Resultsmentioning

confidence: 99%

Glycation of soy protein isolate with two ketoses: d‐Allulose and fructose

Tas

Ertugrul

Mazı

2021

Int J of Food Sci Tech

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Summary Modification of food proteins to have improved functional properties is of great importance. In this study, modification of soy protein isolate (SPI) was achieved through glycation. SPI was glycated in a spray dryer (SD) and an incubator followed by freeze drying (FD). d‐Allulose, an important rare sugar, was used in SPI glycation as the carbohydrate source, and results were compared with fructose. In addition to the sugar type, two different SPI powder: sugar ratios (1:1 and 5:1) were investigated. For the glycated samples, emulsification activity, free amino groups, protein solubility, Fourier‐transform infrared spectroscopy analysis, antioxidant activity experiments and time‐domain NMR relaxometry measurements for hydration were conducted. According to the results, the solubility of SPI that is limited in native form has shown a significant improvement after glycation through both FD and SD methods. Besides, glycation through the FD method was found to be more favourable due to its milder conditions than the SD method. Considering the physicochemical properties, the best combination for the highest glycation degree was found to be the samples prepared at the 1:1 ratio with d‐Allulose in the FD method. Overall, it was concluded that glycation of SPI enhanced its functional properties such as antioxidant and emulsification activities.

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Effects of acylation and glycation treatments on physicochemical and gelation properties of rapeseed protein isolate

Abstract: Acylated and glycated RPI gels were prepared, but the moderate acylation was more favorable to improve the gelation property of RPI.

Cited by 36 publications

References 44 publications

Influences of ultrasonic treatment on structure and functional properties of salt‐soluble protein from Moringa oleifera seeds

Influences of ultrasonic treatment on structure and functional properties of salt‐soluble protein from Moringa oleifera seeds

Relationship between flexibility and interfacial functional properties of soy protein isolate: succinylation modification

Glycation of soy protein isolate with two ketoses: d‐Allulose and fructose

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