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

Abstract

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.

Extraction of Bionanomaterials from the Aqueous Bulk by Using Surface Active and Water-Soluble Magnetic Nanoparticles

“…Gemini surfactant, 12-2-12, was synthesized as reported elsewhere . Wheat and rice proteins samples used in this study were the same samples extracted, characterized, and used in our earlier works. , …”

“…The former proteins are the common food proteins , consisting of predominantly hydrophobic domains with strong amphipathic properties which drive the adsorption of protein on the NP surface to make bionanomaterials. It provides excellent colloidal stabilization to bionanomaterials in the aqueous phase necessary for their versatile biological applications. , …”

“…It provides excellent colloidal stabilization to bionanomaterials in the aqueous phase necessary for their versatile biological applications. 6,7 The extraction ability of magnetic NPs 8−10 depends on their hydrophilic as well as hydrophobic interactions which can be easily controlled by choosing appropriate surfactant stabilized magnetic NPs 11−13 with strong affinity to interact with the hydrophilic and hydrophobic domains of surface adsorbed proteins on Au NPs. Thus, the extraction of protein coated Au NPs from the aqueous bulk depends on the amphiphilic interactions existing between the surfactant stabilized magnetic NPs and the hydrophilic and/or hydrophobic domains of proteins adsorbed on the surface of the Au NPs.…”

“…2 Wheat and rice proteins samples used in this study were the same samples extracted, characterized, and used in our earlier works. 6,15 Hydrothermal Synthesis of Iron Oxide NPs. Iron oxide NPs were synthesized by following the hydrothermal synthesis reported earlier.…”

Proteolysis Degree of Protein Corona Affect Ultrasound-Induced Sublethal Effects on Saccharomyces cerevisiae: Transcriptomics Analysis and Adaptive Regulation of Membrane Homeostasis

“…Notably, wheat glutenin, which accounts for around 45% of the total wheat protein, is a high hydrophobic heterogeneous mixture consisting of various subunits connected by disulfide bonds. Therefore, hydrophobic proteins, similar to conventional hydrophobic surfactants, might be excellent stabilizing agents for nanoparticles [ 12 ].…”