China
Africa
Explore chapters and articles related to this topic
Protein-Based Nanosystems as Emerging Bioavailability Enhancers for Nutraceuticals
Published in Jyoti Ranjan Rout, Rout George Kerry, Abinash Dutta, Biotechnological Advances for Microbiology, Molecular Biology, and Nanotechnology, 2022
Rohini Samadarsi, Debjani Dutta
Gluten-based protein like gliadin is extracted from wheat, which is a dynamic biopolymer mostly suited for oral delivery of bioactive components and nutraceuticals. In addition to the advantages of protein nanoparticles, gliadin has much adhesivity, which is found in polysaccharides like chitosan and greater tropism (indicative growth toward uppermost regions of the gastrointestinal tract and has shown lesser existence toward intestinal region). The hydrophobicity and solubility of gliadin-based nanoparticles can protect the entrapped nutraceutical for its sustained release. For a protein-based nanoparticle, neutral amino acids present in them nurture hydrogen bonding with mucous membranes while lipophilic amino acids present on nanoparticles bind with biological tissue via hydrophobic interactions. Gliadin is rich in both lipophilic and neutral amino acids suggesting that it would have both hydrophobic and hydrogen bonding interactions (Joye et al., 2015; Peng et al., 2017). Peng et al. (2017) developed gliadin-based nanoparticles encapsulated with an anticancer drug for targetting breast cancer cell lines. Gliadin-gelatin-based nanoparticles were also developed with the electrospray technique for the sustained releasing of drugs for cancer therapy.
Applications of Protein Nanoparticles as Drug Delivery Vehicle
Published in Adwitiya Sinha, Megha Rathi, Smart Healthcare Systems, 2019
Reema Gabrani, Ritu Ghildiyal, Neetigyata Pratap, Garima Sharma, Shweta Dang
For oral administration, gliadin is used for drug delivery as it is a gluten protein and possesses bioadhesive properties. It has bioadhesive properties due to its neutral amino acids and shows interaction with intestinal mucosa by hydrogen bonding, and lipophilic amino acids make it suitable for the development of mucoadhesive NPs. The amine and disulfide groups of gliadin protein get attached with the mucin and hence are highly preferred for the synthesis of NPs used for the treatment of gastrointestinal tract. This kind of bioadhesion property can be utilized for the release of anticancer drug in case of colon cancer. The targeted delivery of anticancer drug cyclophosphamide has been delivered by gliadin. In pea seeds, legumin is the storage protein and hence is a good source of sulfur. Therefore, this protein can form NPs due to the self-assembly after the cross-linking process (Lohcharoenkal et al., 2014).
Nanocomposite for Food Packaging
Published in C. Anandharamakrishnan, S. Parthasarathi, Food Nanotechnology, 2019
S.K. Vimala Bharathi, B. Rohini, J.A. Moses, C. Anandharamakrishnan
Gluten is a storage protein that consists of prolamin and glutelin. Alcohol solubilizes prolamin; whereas dilute acids or bases solubilize glutelin (Georgiev and Dekova, 2011). The major sources of gluten are wheat, rye, barley, triticale, and oats. Wheat gluten (Triticum aestivum) is the most commonly used biopolymer and is employed in the form of films and edible coatings. Wheat gluten is composed of gliadin (a prolamin protein) and glutenin (a glutelin protein), which are responsible for viscous properties, and strength and elasticity respectively (Khatkar et al., 1995). Hence, the properties of film vary with gliadin and glutenin ratio. Furthermore, wheat gluten films exhibit lower permeability compared to other films (Telis, 2012).
Quantifying the influence of surface chemical composition on surface energy during powder flow
Published in Particulate Science and Technology, 2021
Camila G. Jange, R. P. Kingsly Ambrose
The low specific energy observed in the butter and gluten systems is due to their lack of polar sites capable of forming intermolecular hydrogen bonds. The carboxylic acid in triacylglycerol (fatty) molecules is the only polar site that possesses the ability of hydrogen-bond formation due to the presence of a basic moiety (C = O). The coil structure and the disulfide covalent bonds intermediating gliadin and glutenin molecules in gluten systems favor strong intramolecular hydrogen and ionic bonds over strong intermolecular pair-electron interactions (Shewry et al. 2002). Shah et al. (2017) also observed changes in the specific component of surface energy due to the differences in group functionalities and electronegativity of haloalkanes. It is also important to emphasize that the higher specific surface area may have contributed to a rise in the net surface energy of the control and starch-coated systems (Table 2).
Ozone: An Advanced Oxidation Technology for Starch Modification
Published in Ozone: Science & Engineering, 2019
R. Pandiselvam, M.R. Manikantan, V. Divya, C. Ashokkumar, R. Kaavya, Anjineyulu Kothakota, S.V. Ramesh
Treatment of ozone on the deproteinization of starch granules increases the degree of oxidation (Chan et al. 2011). The authors stated that the resident starches exhibit higher carboxylic content as compared to deproteinized starch and also deproteinization causes reduction in pasting viscosity. These types of changes can prove that the presence of protein, polyphenols, and nonstarch polysaccharides reduces the effect of ozone on starch granules, this modified starch molecule not as much reactive like unmodified grains molecules. Obadi and co-workers (2016) examined the effects of ozone gas at 5 g/h for 0–60 min exposure on wheat gluten, glutenin, and gliadin properties. It was found that exposing wheat proteins to ozone gas for 60 min deteriorated the quality of wheat protein. Li, Guan, and Bian (2014) used ozone at 80 mg/L to treat the wheat grains for 4 h. The authors observed that the wet gluten content decreased and the gluten index increased after the treatment. Goze et al. (2016) evaluated the effect of ozone treatment on the wheat proteins and its impact on bread making. The profound changes in prolamin class wheat proteins showed an impact on the increased tenacity and limitation to extensibility of the flours or doughs obtained after ozonation. Obadi et al. (2018) analyzed the structural and microscopic structure of ozone-treated flour and showed significant changes in the side chains of protein and fats of the whole grain flour. In contrast to this, Felipe et al. (2016) reported that the ozonation process did not change the dry or wet gluten content of wheat grains.
Pickering-stabilized emulsion gels fabricated from wheat protein nanoparticles: Effect of pH, NaCl and oil content
Published in Journal of Dispersion Science and Technology, 2018
Yu Qing Zhu, Xing Chen, David Julian McClements, Liqiang Zou, Wei Liu
Pickering-stabilized emulsion gels with different oil contents, pH values, and ionic strengths were prepared. Initially, gliadin nanoparticle dispersions were diluted to a protein content of 1% w/w. The nanoparticle dispersions were then adjusted to different pH and ionic strength values by adding acid/base (HCl/NaOH) or salt (NaCl) with oil content fixed at 50%. Pickering-stabilized emulsion gels with different oil contents (30 − 70% w/w) were prepared by blending corn oil and protein nanoparticle dispersions together using a high-shear mixer (ULTRA TURRAX® T18 digital, IKA, Staufen, Germany) with a 19 mm dispersion head operating at 12,000 rpm for 2 min in the absence of NaCl at pH 5.0. The type of Pickering-stabilized emulsion gels formed (O/W or W/O) was determined by checking their miscibility in water or corn oil: O/W emulsions tend to disperse easily in water but not in oil, whereas W/O emulsions do the opposite.