Synthesis and Characterization of Various Protein α-Lactalbumin Nanotubes Structures by Chemical Hydrolysis Method


New water-based nanofluids including unparalleled milk protein α-lactalbumin hollow nano-bio-tubes using low cost, available and advanced partial chemical hydrolysis strategy in bottom-up nano-assembly have been employed in this work. The aqueous sol-gel chemistry in nanotechnology which we selected for this goal offers new fabrication as interesting smart protein nanotubes. The kinds of nanometer sized tubular structures such as waved, helically coiled, bent, bamboo-shaped, bead-like and branched single-walled protein nanotubes (SWPNTs) with a range of 3 - 8 nm in outer diameters were produced by this method. Complete characterization for natural produced nanotubes including SEM, TEM images, G bond and D bond in Raman spectroscopy, XRD patterns, DLS (Dynamic Light Scattering) and FTIR analysis were evaluated which they are most significant experiments in synthesized protein nanotubes soluble in clear water nanofluids and stabilization of transparent nanofluids was proved within more than one year after preparation. Various necessary ligand ion salts such as Mn2+, Zn2+ and Ca2+ or mixtures as bridge makers and producing biological self-assembly hollow SWPNTs were performed and we focused on new chemical technology under specific acidic hydrolysis method not conventional enzymatic proteolysis and applying surfactants, pH reagent, Tris-HCl buffer, polar solvent which could be produced by β-sheet stacked hydrolysed protein α-lactalbumin mechanism under appropriate conditions to achieving high efficiency new protein nanotubes skeleton. They can be promising materials applied in food science, diet nutrition, nanomedicine, nano-biotechnology and surgery.

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Esmaeilzadeh, P. , Fakhroueian, Z. , Esmaeilzadeh, P. and Mohammadi, N. (2013) Synthesis and Characterization of Various Protein α-Lactalbumin Nanotubes Structures by Chemical Hydrolysis Method. Advances in Nanoparticles, 2, 154-164. doi: 10.4236/anp.2013.22024.

Conflicts of Interest

The authors declare no conflicts of interest.


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