Thermal protection of β-carotene in re-assembled casein micelles during different processing technologies applied in food industry

Sáiz-Abajo, María-José; González-Ferrero, Carolina; Moreno-Ruiz, Ana; Romo-Hualde, Ana; González-Navarro, Carlos J.

doi:10.1016/j.foodchem.2012.11.016

Cited by 162 publications

(62 citation statements)

References 43 publications

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“…3 Studies have demonstrated that b-CE exhibits several biological functions, for example as an anticancer agent and antioxidant, and in the prevention of cardiovascular diseases. Among these carotenoids, b-carotene (b-CE), with its antioxidant properties, is the most widespread.…”

Section: Introductionmentioning

confidence: 99%

“…Among these carotenoids, b-carotene (b-CE), with its antioxidant properties, is the most widespread. 6 To solve the abovementioned problems, various potential technologies, including encapsulation, 7 nanoemulsication 6 and self-assembly, 3 have been introduced to improve the utilization, bioaccessibility and stability of b-CE in foods. 3 Studies have demonstrated that b-CE exhibits several biological functions, for example as an anticancer agent and antioxidant, and in the prevention of cardiovascular diseases.…”

Section: Introductionmentioning

confidence: 99%

“…11 Semo et al suggested that CN can re-assemble in vitro and have a strong tendency to bind hydrophobic molecules, still exhibiting similar properties to those of the originally occurring CN micelles (CM). 3 CN has also been used to deliver drugs in medical applications. Re-assembled CM could encapsulate and deliver vitamin D2, and be used as a nano-delivery system to protect against photochemical degradation of the vitamin.…”

Section: Introductionmentioning

confidence: 99%

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Characterization and bioaccessibility of β-carotene in re-assembled casein

Zhang

et al. 2015

RSC Adv.

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The characterization and bioaccessibility of b-carotene (b-CE) in re-assembled casein (CN) were investigated in this study. At pH 4.6, b-CE in re-assembled CN significantly lowered the zeta-potential to a negative value compared to that of CN. The morphology of b-CE in re-assembled CN was characterized by atomic force microscopy. b-CE in re-assembled CN exhibited a more uniform and homogenous dispersion, with peak-to-valley differences of 6.8 nm rather than 91.3 nm for the pure b-CE. b-CE in re-assembled CN can effectively protect b-CE against degradation under conditions of heat and ultraviolet radiation. The antioxidant activity of b-CE when it was encapsulated in re-assembled CN was significantly higher than b-CE in control samples under both experimental conditions. The total release rate of b-CE was 76.7% and 63.4% by trypsin and pepsin hydrolysis, respectively. These results indicated a feasible application in the food industry.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Characterization and bioaccessibility of β-carotene in re-assembled casein

Zhang

et al. 2015

RSC Adv.

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“…Furthermore, different casein nanoparticles were shown to protect the content against cold storage, heat, high hydrostatic pressure processing, oxidation and ultraviolet (UV) radiation [40, 74, 77, 80, 82]. Nonetheless, reassembled casein nanoparticles are readily digested by gastrointestinal proteases [79–81].…”

Section: Casein Delivery Particlesmentioning

confidence: 99%

Potential of Casein as a Carrier for Biologically Active Agents

2017

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Casein is the collective name for a family of milk proteins. In bovine milk, casein comprises four peptides: αS1, αS2, β, and κ, differing in their amino acid, phosphorus and carbohydrate content but similar in their amphiphilic character. Hydrophilic and hydrophobic regions of casein show block distribution in the protein chain. Casein peptides carry negative charge on their surface as a result of phosphorylation and tend to bind nanoclusters of amorphous calcium phosphate. Due to these properties, in suitable conditions, casein molecules agglomerate into spherical micelles. The high content of casein in milk (2.75 %) has made it one of the most popular proteins. Novel research techniques have improved understanding of its properties, opening up new applications. However, casein is not just a dietary protein. Its properties promise new and unexpected applications in science and the pharmaceutical and functional food industries. One example is an encapsulation of health-related substances in casein matrices. This review discusses gelation, coacervation, self-assembly and reassembly of casein peptides as means of encapsulation. We highlight information on encapsulation of health-related substances such as drugs and dietary supplements inside casein micro- and nanoparticles.

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“…In their native state, caseins usually exist as molecular clusters ("casein micelles") that are typically between about 50 and 250 nm in diameter and are partly held together by mineral ions (such as calcium phosphate). Casein micelles may be useful for the development of delivery systems because they can encapsulate lipophilic bioactives in their non-polar interiors, such as carotenoids, curcumin, and oil-soluble vitamins [83][84][85][86]. Caseins are amphiphilic molecules that have good surface-activity and can therefore be used as emulsifiers to stabilize lipid droplets.…”

Section: Caseinmentioning

confidence: 99%