In this work, we investigated the photo-degradation performance of MnO2-SiC fiber-TiO2 (MnO2-SiC-TiO2) ternary nanocomposite according to visible light excitation utilizing methylene blue (MB) and methyl orange (MO) as standard dyes. The photocatalytic physicochemical characteristics of this ternary nanocomposite were described by X-ray diffraction (XRD), scanning electron microscopy (SEM), tunneling electron microscopy (TEM), ultraviolet-visible (UV-vis), diffuse reflectance spectroscopy (DRS), electrochemical impedance spectroscopy (EIS), photocurrent and cyclic voltammogram (CV) test. Photolysis studies of the synthesized MnO2-SiC-TiO2 composite were conducted using standard dyes of MB and MO under UV light irradiation. The experiments revealed that the MnO2-SiC-TiO2 exhibits the greatest photocatalytic dye degradation performance of around 20 % with MB, and of around 10 % with MO, respectively, within 120 min. Furthermore, MnO2-SiC-TiO2 showed good stability against photocatalytic degradation. The photocatalytic efficiency of the nanocomposite was indicated by the adequate photocatalytic reaction process. These research results show the practical application potential of SiC fibers and the performance of a photocatalyst composite that combines these fibers with metal oxides.

Porcine parvovirus (PPV), a member of the genus Parvovirus, family Parvoviridae, is a significant causative agent in porcine reproductive failure, causing serious economic losses in the swine industry. PPV is a non-enveloped virus and its capsid is assembled from three viral proteins (VP1, VP2, and VP3). The major capsid protein, VP2 is the main target for neutralizing antibodies in PPV. When VP2 was expressed in large amounts, it assembled into virus-like particles (VLPs) similar in size and morphology to the original virions. In this study, we generated the recombinant Bombyx mori nucleopolyhedrovirus (BmNPV) to express the VP2 protein. Expression of the VP2 protein was analyzed by SDS-PAGE and Western blot. The recombinant VP2 protein of approximately 64 kDa was detected by both analyses. The formation of VLP by recombinant VP2 was confirmed through transmission electron microscopy examination. The purified VP2 protein assembled into spherical particles with diameters ranging from 20 to 22 nm.