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      Potential of Casein as a Carrier for Biologically Active Agents

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          Abstract

          Casein is the collective name for a family of milk proteins. In bovine milk, casein comprises four peptides: α S1, α S2, 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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          Terminology for biorelated polymers and applications (IUPAC Recommendations 2012)

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            Earliest evidence for cheese making in the sixth millennium BC in northern Europe.

            The introduction of dairying was a critical step in early agriculture, with milk products being rapidly adopted as a major component of the diets of prehistoric farmers and pottery-using late hunter-gatherers. The processing of milk, particularly the production of cheese, would have been a critical development because it not only allowed the preservation of milk products in a non-perishable and transportable form, but also it made milk a more digestible commodity for early prehistoric farmers. The finding of abundant milk residues in pottery vessels from seventh millennium sites from north-western Anatolia provided the earliest evidence of milk processing, although the exact practice could not be explicitly defined. Notably, the discovery of potsherds pierced with small holes appear at early Neolithic sites in temperate Europe in the sixth millennium BC and have been interpreted typologically as 'cheese-strainers', although a direct association with milk processing has not yet been demonstrated. Organic residues preserved in pottery vessels have provided direct evidence for early milk use in the Neolithic period in the Near East and south-eastern Europe, north Africa, Denmark and the British Isles, based on the δ(13)C and Δ(13)C values of the major fatty acids in milk. Here we apply the same approach to investigate the function of sieves/strainer vessels, providing direct chemical evidence for their use in milk processing. The presence of abundant milk fat in these specialized vessels, comparable in form to modern cheese strainers, provides compelling evidence for the vessels having being used to separate fat-rich milk curds from the lactose-containing whey. This new evidence emphasizes the importance of pottery vessels in processing dairy products, particularly in the manufacture of reduced-lactose milk products among lactose-intolerant prehistoric farming communities.
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              pH-driven encapsulation of curcumin in self-assembled casein nanoparticles for enhanced dispersibility and bioactivity.

              The poor water solubility and bioactivity of lipophilic phytochemicals can be potentially improved by delivery systems. In this study, a low-cost, low-energy, and organic solvent-free encapsulation technology was studied by utilizing the pH-dependent solubility properties of curcumin and self-assembly properties of sodium caseinate (NaCas). Curcumin was deprotonated and dissolved, while NaCas was dissociated at pH 12 and 21 °C for 30 min. The subsequent neutralization enabled the encapsulation of curcumin in self-assembled casein nanoparticles. The degradation of curcumin under encapsulation conditions was negligible based on visible light and nuclear magnetic resonance spectroscopy. The dissociation of NaCas at pH 12 and reassociation after neutralization were confirmed using dynamic light scattering and analytical ultracentrifugation. The curcumin encapsulated in casein nanoparticles showed significantly improved anti-proliferation activity against human colorectal and pancreatic cancer cells. The studied encapsulation method is promising to utilize lipophilic compounds in food or pharmaceutical industries.
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                Author and article information

                Contributors
                +48 34 361 41 18 , tomasz.glab@ajd.czest.pl
                +48 71 370 99 80 , borat@iitd.pan.wroc.pl
                Journal
                Top Curr Chem (J)
                Top Curr Chem (J)
                Topics in Current Chemistry (Journal)
                Springer International Publishing (Cham )
                2365-0869
                2364-8961
                15 July 2017
                15 July 2017
                2017
                : 375
                : 4
                : 71
                Affiliations
                [1 ]ISNI 0000 0001 1931 5342, GRID grid.440599.5, Department of Biomedical Sciences, Faculty of Mathematics and Natural Sciences, , Jan Dlugosz University in Czestochowa, ; 13/15 Armii Krajowej Avenue, 42-200 Czestochowa, Poland
                [2 ]ISNI 0000 0001 1958 0162, GRID grid.413454.3, Laboratory of Biomedical Chemistry “NeoLek”, Hirszfeld Institute of Immunology and Experimental Therapy, , Polish Academy of Sciences, ; 12 Rudolf Weigl Street, 53-114 Wroclaw, Poland
                Article
                158
                10.1007/s41061-017-0158-z
                5511616
                28712055
                8d2e2eee-18e1-49c9-a520-6d0b13a4e1a9
                © The Author(s) 2017

                Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License ( http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

                History
                : 6 April 2017
                : 29 June 2017
                Categories
                Review
                Custom metadata
                © Springer International Publishing AG 2017

                casein,milk proteins,encapsulation,release,delivery,carriers
                casein, milk proteins, encapsulation, release, delivery, carriers

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