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Corn Zein

The biocompatibility of zein nanoparticles was exploited for the development of fluorescent nanoparticles. Zein nanoparticles were made fluorescent by the addition of ZnS Mn quantum dots for nanoscale delivery of 5-Huoruracil was proposed (Aswathy et al., 2012). These multifunctional nanoparticles could be used for delivery of drugs and imaging the cancer cells. [Pg.605]

The formation of microspheres from various pectin hydrogel complexes and corn zein in the presence of calcium and zinc ions has been proposed (Mukhidinov et al., 2011). It is shown that the formation of microspheres and their loading capacity for a drug (piroxicam) depend on the type of biopolymers, their ratio, the sizes of the bivalent ions, and the molecular mass of the pectin. It was supposed that complexes of pectin with zein would suppress pectin swelling in the stomach and, thereby, limit drug degradation in the GI tract. [Pg.605]

Biodegradable, tetracycline-loaded microparticles made of two polymers, poly lactide-co-glycolic and zein, which were compressed into monolithic devices and proposed in the treatment with antibiotics within the periodontal pocket against bacterial infections (Oliveira de Sousa et al., 2011). Sustained release of tetracycline was obtained, and the proportion of zein in the inserts had a great impact on the drug release. [Pg.605]

Wheat gluten (WG) is a general term for water-insoluble proteins of wheat flour, which is composed of a mixture of polypeptide molecules, considered to be globular proteins. The proteins are [Pg.605]

More recently, succinic acid deamidated wheat gluten microspheres for encapsulation of fish oil via O/W/0 doubleemulsion followed by heat-polymerization of emulsified WG was reported (Liao et al., 2012). During microspheres formation, dramatically elevated intermolecular a regation caused the formation of a compact network structure of succinic acid deamidated WG molecules, in which fish oil was encapsulated. Heat-pol5mierization at the same time increased interactions (hydrogen bonds and hydrophobic interactions) between the two components. [Pg.606]


Gliadins are prolamins, a group of plant storage proteins with a high proline content, found in the seeds of cereal grains wheat (gliadin), barley (hordein), rye (secalin), corn (zein) and, as a minor protein, avenin in oats. [Pg.89]

Robert Boyer of H. Ford s Edison Institute was awarded an important patent in 1945 (Boyer et al., 1945) for producing textile fibers from soybean meal for use in automobile upholstery. In addition to soy protein, casein, corn zein, and peanut protein were also used to produce regenerated protein fibers. H. Ford once wore a suit made from soy protein fibers, which was reportedly quite itchy when dry and odiferous when wet. Soy protein fiber technology never attained commercial textile production... [Pg.563]

Blending with corn zein protein can strengthen soy protein fibers. Soy—zein blends exhibited increased tenacity and more flexibility. As with soy protein fibers, properties of blended fibers changed with water activity, but the properties were always better with blended fiber systems (Zhang et al., 1997). [Pg.565]

Proteins, e.g., collagen, gelatin, corn zein. - Often based on terephthallc acid, e.g.. [Pg.223]

Protein-based plastics have been used, alone or in mixtures, to obtain edible films and eoatings. They have been used to protect pharmaceuticals and to improve the shelf life of food products. Some commercialization of protein films has been realized in collagen sansage casing, gelatin pharmaceutical capsules and corn zein protective coatings for nutmeats and candies [71]. [Pg.52]

The film-forming properties of corn zein have also been investigated in detail [2, 44-55]. Zein films are water-insoluble, relatively shiny and greaseproof, but they sometimes have unsuitable organoleptic properties (off-odour, chewiness and so on). Zein-based films and coatings improve food shelf life, via their high barrier properties (to water vapour or especially to oxygen (O2)), or their retention or controlled release properties of active additives on the food surface. These films have been successfully used to protect dry fruits and various parts of frozen or intermediate moisture foods. [Pg.379]

The nse of albnmen proteins as a base for the encapsnlation of hydrophobic organic componnds for cosmetic or food uses is the focus of several patents [120-122]. Application of albumen coatings can reduce raisin moisture loss in breakfast mixtures [123]. Albumen has also been used as an edible coating ingredient [124, 126]. Okamoto [83] reported the formation of films on the surface of heated albumen-based lipoprotein solutions, similar to the formation of soy films. The mechanical and water vapour properties of albumen-based films were studied by Gennadios and co-workers [125]. The materials are clearer and more transparent than wheat gluten-, soy protein- and corn zein-based materials. Albumen-based films could be... [Pg.381]

Wheat gluten + 10% glycerol Wheat gluten + 30% glycerol Wheat gluten + 30% glycerol + 15 min at 130°C Corn zein proteins ... [Pg.341]

Sodium caseinate Soy proteins - pH 3 Corn zein HPMC... [Pg.342]

Vicara (corn zein-based fibres) Casein textiles... [Pg.341]

Most proteins (see Table 11.9 for their structure) have been used in food sciences, but recently a number of proteins of plant origin have received attention for the production of biodegradable polymers. These proteins include corn zein, wheat gluten, soy protein, and sunflower protein. The major drawback of protein-based plastics, apart from keratin, is... [Pg.361]


See other pages where Corn Zein is mentioned: [Pg.1375]    [Pg.320]    [Pg.114]    [Pg.3349]    [Pg.191]    [Pg.2]    [Pg.569]    [Pg.711]    [Pg.408]    [Pg.202]    [Pg.197]    [Pg.431]    [Pg.377]    [Pg.382]    [Pg.384]    [Pg.388]    [Pg.397]    [Pg.127]    [Pg.337]    [Pg.343]    [Pg.347]    [Pg.351]    [Pg.351]    [Pg.353]    [Pg.357]    [Pg.364]    [Pg.368]    [Pg.399]    [Pg.128]    [Pg.228]    [Pg.459]    [Pg.604]   


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