The room-temperature epitaxial growth of ZnO thin films on NiO buffered sapphire (0001) substrate was achieved by using the laser molecular-beam-epitaxy method. The obtained ZnO films had the ultrasmooth surface reflecting the nanostepped structure of the sapphire substrate. The crystal structure at the surface was investigated in situ by means of coaxial impact-collision ion scattering spectroscopy. It was proved that the buffer-enhanced epitaxial ZnO thin films grown at room temperature had +c polarity, while the polarity of high-temperature grown ZnO thin films on the sapphire was −c. Photoluminescence spectra at room temperature were measured for the epitaxial ZnO films, showing only the strong ultraviolet emission near 380nm.

We investigated atomic-scale surface modifications of silicate glass by nanoimprint using an atomically stepped sapphire (α-Al2O3 single crystal) plate as nanopattern mold. The sapphire mold had regularly arranged straight atomic steps, with uniform height and terrace width of about 0.2 and 80 nm, respectively. During pressing, vertical positions of the sapphire mold and glass plate significantly affected the morphology of the imprinted glass surface. The nanopattern was transferred to the glass surface when the mold was set on the glass plate, while the nanowave pattern was formed on the glass surface when the glass plate was set on the mold.

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Room-temperature epitaxy of AlN thin films on sapphire (0001) substrates was achieved by pulsed laser deposition using an epitaxial NiO ultrathin buffer layer (approximately 6 nm thick). Four-circle x-ray diffraction analysis indicates a double heteroepitaxial structure of AlN (0001)/NiO(111)/sapphire (0001) with the epitaxial relationship of AlN [10-10] ‖ NiO [11-2] ‖ sapphire [11-20]. The surface morphology of room-temperature grown AlN thin films was found to be atomically smooth and nanostepped, reflecting the surface of the ultrasmooth sapphire substrate with 0.2-nm-high steps.

Antioxidant activities against hypochlorite ions and peroxyl radicals of a chicken dark meat hydrolysate digested with pepsin were examined with the myoglobin method based on the structure change of myoglobin due to redox reaction with reactive oxygen species (ROS). A peptide that showed strong antioxidant activity against the peroxyl radical was isolated from the hydrolysate using HPLC equipped with a hydrophobic-interacting column. The sequence of the first five amino acid residues of the peptide was determined as YASGR (Tyr-Ala-Ser-Gly-Arg), and this sequence matched with the amino acid residues 143-147 of chicken β-actin (GenBank: CAA25004.1). The synthetic peptide YASGR showed very high antioxidant activity against the peroxyl radical. Antioxidant activities of the free amino acids, confirmed that the tyrosine residue of this peptide was possibly responsible for antioxidant activity.