Role of Gluten in Surface Chemistry: Nanometallic Bioconjugation of Hard, Medium, and Soft Wheat Protein.

Hard, medium, and soft wheat proteins, based on gluten content, were studied for their important roles in nanometallic surface chemistry. In situ synthesis of Au nanoparticles (NPs) was followed to determine the surface adsorption behavior of wheat protein based on the gluten contents. A greater amount of gluten contents facilitated the nucleation to produce Au NPs. X-ray photoelectron spectroscopy (XPS) surface analysis clearly showed the surface adsorption of protein on nanometallic surfaces which was almost equally prevalent for the hard, medium, and soft wheat proteins. Wheat protein conjugated NPs were highly susceptible to phase transfer from aqueous to organic phase that was entirely related to the amount of gluten contents. The presence of higher gluten content in hard wheat protein readily enabled the hard wheat protein conjugated NPs to move across the aqueous-organic interface followed by medium and soft wheat protein conjugated NPs. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS page) analysis allowed us to determine molar masses of nanometallic surface adsorbed protein fractions. Only two protein fractions of high molar masses (74 and 85 kDa) from SDS solubilized hard, medium, and soft wheat proteins preferred to adsorb on nanometallic surfaces out of more than 15 protein fractions of pure wheat protein. This made the surface adsorption of wheat protein highly selective and closely related to gluten content. Cetyltrimethylammonium bromide (CTAB) solubilized wheat protein conjugated NPs demonstrated their strong antimicrobial activities against both Gram negative and Gram positive bacteria making them suitable for their applications in food industry.

Applications of rice protein in nanomaterials synthesis, nanocolloids of rice protein, and bioapplicability.

Rice protein conjugated nanomaterials were synthesized and characterized by using anionic and cationic forms of rice protein. Both forms showed unique characteristic features when used in in situ reaction conditions for synthesizing the protein stabilized gold (Au) and silver (Ag) nanoparticles (NPs). Au NPs synthesis was highly facilitated than Ag NPs synthesis while the reverse was true when rice protein was simply used in the basic medium. Photophysical behavior clearly showed the contributions of both electrostatic and non-electrostatic interactions driving the rice protein surface adsorption on nanometallic surfaces. Rice protein conjugated NPs were easily transferred and extracted into the organic phase while the extraction process was related to the amount of protein coating. Under the controlled pH reaction conditions, rice protein - dye colored NPs were synthesized which were further characterized by the DLS and SDS Page analysis. Both rice protein conjugated Au/Ag NPs and rice protein NPs showed remarkable biocompatibility with blood cells. These NPs demonstrated their excellent ability to selectively extract protein fractions from complex biological fluid like serum. The results proposed significant applications of rice protein conjugated NPs in biological systems as well as bio-nanotechnology.

Naringin-Chalcone Bioflavonoid-Protected Nanocolloids: Mode of Flavonoid Adsorption, a Determinant for Protein Extraction.

In order to highlight the applications of bioflavonoids in materials chemistry, naringin and its chalcone form were used in the nanomaterial synthesis to produce flavonoid-conjugated nanomaterials in aqueous phase. Chalcone form proved to be excellent reducing as well as stabilizing agent in the synthesis of monodisperse Au, Ag, and Pd nanoparticles (NPs) of ∼5-15 nm, following in situ reaction conditions where no external reducing or stabilizing agents were used. The mechanism of NP surface adsorption of flavonoid was determined with the help of dynamic light scattering and zeta potential measurements. Surface-adsorbed flavonoids also allowed NPs to easily transfer into the organic phase by using aqueous insoluble ionic liquid. Pd NPs attracted the excessive amount of surface adsorption of both naringin as well as its chalcone form that in turn drove Pd NPs in self-assembled state in comparison to Au or Ag NPs. An amount of surface-adsorbed flavonoids selectively determined the extraction of protein fractions from complex zein corn starch protein solution. Self-assembled Pd NPs with a large amount of surface-adsorbed naringin preferentially extracted zein fraction of higher molar mass, whereas Au and Ag NPs almost equally extracted the zein fractions of lower molar masses.