Interactions of blueberry anthocyanins with whey protein isolate and bovine serum protein: Color stability, antioxidant activity, in vitro simulation, and protein functionality

Zang, Zhihuan; Chou, Shurui; Geng, Lin; Si, Xu; Ding, Yumeng; Lang, Yuxi; Cui, Hong; Gao, Ningxuan; Chen, Yi; Wang, Mingshuang; Xie, Xu; Xue, Bin; B, Li; Tian, Jinlong

doi:10.1016/j.lwt.2021.112269

Cited by 45 publications

(29 citation statements)

References 37 publications

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“…However, with a longer storage time, a higher color difference was noticed in the BSA–CS‐stabilized emulsion than in the WPI–CS counterpart ( p < 0.05). This could be plausibly due to the different levels of pigments or other components used in both emulsions, particularly proteins, which were from different origins (Zang et al., 2021). Thus, CS not only stabilized the emulsion but also helped to prevent oxidation of SO and astaxanthin (Rajasekaran et al., 2022).…”

Section: Resultsmentioning

confidence: 99%

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Combined effect of chitosan and bovine serum albumin/whey protein isolate on the characteristics and stability of shrimp oil‐in‐water emulsion

Rajasekaran

Singh

Benjakul

2022

Journal of Food Science

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The effect of bovine serum albumin (BSA) or whey protein isolate (WPI) at various concentrations (0.5%, 1.5%, and 3%; w/v) on the properties of shrimp oil-in-water emulsion was investigated. Both proteins at 1.5% showed the highest emulsifying properties. Moreover, the combined impact of chitosan (CS) at different levels (0.25%, 0.50%, 0.75%, and 1%; w/v) and 1.5% BSA or 1.5% WPI on emulsion properties was also studied. For the same protein used, those stabilized by BSA and WPI in conjunction with CS solution at 0.5% and 0.25% had the highest emulsion stability index, respectively. During storage for 28 days, the BSA-CSstabilized emulsion had higher turbidity, a*, b* but the lowest L* values compared to the WPI-CS counterpart (p < 0.05). Emulsion stabilized by the BSA-CS complex showed higher stability, as witnessed by lower d 32 and d 43 and lower flocculation factor and coalescence index, but it had a lower negative charge than those stabilized by the WPI-CS complex (p < 0.05). Oil droplets of the BSA-CS-stabilized emulsion showed a lower extent of size enlargement after storage. Rheological studies revealed viscous, shear-thinning, and non-Newtonian behavior of emulsions. Overall, emulsion stabilized by the BSA-CS complex had higher stability than that stabilized by the WPI-CS complex, and the former could maintain the stability of pigment in shrimp oil to some extent. K E Y W O R D Sbovine serum albumin, chitosan, emulsion, hepatopancreas, shrimp oil, whey protein isolate Practical Application: Oil from shrimp hepatopancreas is a rich source of both astaxanthin and polyunsaturated fatty acids with health benefits. It can be used for the preparation of food emulsion, such as mayonnaise, with nutraceutical properties. However, emulsion stability determines the quality of the emulsion.The use of protein (bovine serum albumin) in conjunction with polysaccharides, especially chitosan at appropriate concentrations, was proven to improve shrimp oil-in-water emulsion during extended storage. Additionally, chitosan can act as an antioxidant to prevent the degradation of astaxanthin to some extent. This finding could be potentially beneficial to produce emulsion with high stability using protein-chitosan complexes.

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Section: Resultsmentioning

confidence: 99%

“…The increased emulsifying properties with the addition of CS at the proper level might be associated with the formation of a protein‐CS complex at the interface. Normally, BSA has higher surface hydrophobicity than WPI (Zang et al., 2021). Therefore, BSA had a greater number of binding sites, leading to a higher interaction with oil droplets.…”

Section: Resultsmentioning

confidence: 99%

Combined effect of chitosan and bovine serum albumin/whey protein isolate on the characteristics and stability of shrimp oil‐in‐water emulsion

Rajasekaran

Singh

Benjakul

2022

Journal of Food Science

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“…Recently, binding of anthocyanins to whey and other dietary proteins has been a strategy to improve the color, antioxidant capacity, stability, bioavailability, and assorted additional functional properties of the pigment as an ingredient in functional products. ,− When bound to proteins, the polyphenols effectively blunt the reactive properties of some proteins (e.g., tendency to self-aggregate or bind to other molecules), which would otherwise trigger destabilizing events, and the proteins protect the anthocyanins from color changes and loss of antioxidant capacity in the food matrix. ,, Similarly, because binding is driven by a combination of electrostatic and hydrogen bonding, the oxidative reactivity of polyphenols can be modified as a result of non-covalent binding to proteins. In combination, these interactions serve to stabilize the targeted anthocyanins.…”

Section: Application Of Protein–polyphenol Aggregate Particlesmentioning

confidence: 99%

Boosting the Bioaccessibility of Dietary Bioactives by Delivery as Protein–Polyphenol Aggregate Particles

Lila

Hoskin

Grace

et al. 2022

J. Agric. Food Chem.

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Protein–polyphenol aggregate particles concurrently fortify a functional food product with healthy dietary proteins and concentrated polyphenols. However, what impact does ingestion of aggregate particles have on ultimate health relevance of either the polyphenolic molecules in the matrix or the protein molecules? Because human health benefits are contingent on bioavailability after ingestion, the fate of these molecules during transit in the gastrointestinal tract (GIT) will dictate their utility as functional food ingredients. This brief review explores diverse applications of protein–polyphenol particles in the food industry and the bioaccessibility of both bioactive polyphenolic compounds and edible proteins. Evidence to date suggests that complexation of phytoactive polyphenolics effectively enhances their health-relevant impacts, specifically because the phytoactives are protected in the protein matrix during transit in the GIT, allowing intact, non-degraded molecules to reach the colon for catabolism at the gut microbiome level, a prerequisite to realize the health benefits of these active compounds.

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“…Polyphenols are highly reactive and easily interact with the active part of protein molecules to form complexes, thus affecting the structural and functional properties of the protein [ 4 , 9 ]. It has been reported that anthocyanins, gallic acid, chlorogenic acid and epigallocatechin gallate lead to significant improvements in the emulsification properties of WPI [ 4 , 10 , 11 ]. Zhong et al [ 12 ] found that the rheological properties of WPI-puerarin hydrogels could be changed by different levels of polyphenol; in particular, the complex shear modulus and hardness of the hydrogels increased when the puerarin content increased.…”

Section: Introductionmentioning

confidence: 99%

The Effects of Ethanol and Rutin on the Structure and Gel Properties of Whey Protein Isolate and Related Mechanisms

Jia

Lin

et al. 2022

Foods

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The effects of different levels of rutin (0, 0.05%, 0.1%, 0.2% and 0.3% w/v) and ethanol on the structure and gel properties of whey protein isolate (WPI) were examined. The results showed that the addition of ethanol promoted the gel formation of WPI. The addition of rutin increased the gel strength of WPI and maintained the water-holding capacity of the gel. Ethanol caused an increase in thiol content and surface hydrophobicity, but rutin decreased the thiol content and surface hydrophobicity of WPI. The particle size, viscosity and viscoelasticity of WPI increased at rutin levels of 0.2% and 0.3%, indicating that rutin caused cross-linking and aggregation of WPI, but rutin had no significant effect on the zeta-potential, indicating that electrostatic interactions were not the main force causing the changes in protein conformation and gel properties. Ethanol and rutin improved the gel properties of WPI possibly by inducing cross-linking of WPIs via hydrophobic and covalent interactions.

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Interactions of blueberry anthocyanins with whey protein isolate and bovine serum protein: Color stability, antioxidant activity, in vitro simulation, and protein functionality

Cited by 45 publications

References 37 publications

Combined effect of chitosan and bovine serum albumin/whey protein isolate on the characteristics and stability of shrimp oil‐in‐water emulsion

Combined effect of chitosan and bovine serum albumin/whey protein isolate on the characteristics and stability of shrimp oil‐in‐water emulsion

Boosting the Bioaccessibility of Dietary Bioactives by Delivery as Protein–Polyphenol Aggregate Particles

The Effects of Ethanol and Rutin on the Structure and Gel Properties of Whey Protein Isolate and Related Mechanisms

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