In this work, the photocatalytic property of p-type CuO was tailored by creating a heterojunction with n-type CdS. The CuO/CdS nanocomposite photocatalyst was synthesized by the ultrasound-assisted-wet-impregnation method and the physicochemical and optical properties of the catalysts were evaluated by using N2 physisorption, X-Ray Diffraction (XRD),X-Ray Photoelectron Spectroscopy (XPS), Raman spectroscopy, Transmission electron microscopy (TEM), Energy dispersive X-Ray (EDX) mapping, Field Emission Scanning Electron Microscope (FE-SEM), UV-Vis and photoluminescence spectroscopy experiments. Detailed characterization revealed the formation of a nanocomposite with a remarkable improvement in the charge carrier (electron/hole) separation. The photocatalytic degradation efficiencies of CuO and CuO/CdS were investigated for different dyes, for instance, rhodamine B (RhB), methylene blue (MLB), methyl blue (MB) and methyl orange (MO) under visible light irradiation. The obtained dye degradation efficiencies were ~93%, ~75%, ~83% and ~80%, respectively. The quantum yield for RhB degradation under visible light was 6.5 × 10-5. Reusability tests revealed that the CuO/CdS photocatalyst was recyclable up to four times. The possible mechanisms for the photocatalytic dye degradation over CuO/CdS nanocomposite were elucidated by utilizing various scavengers. Through these studies, it can be confirmed that the conduction band edges of CuO and CdS play a significant role in producing O2-. The produced O2- degraded the dye molecules in the bulk solution whereas the valence band position of CuO acted as the water oxidation site. In conclusion, the incorporation of CuO with CdS was demonstrated to be a viable strategy for the efficient photocatalytic degradation of dyes in aqueous solutions.
A novel thermostable glucoamylase cDNA without starch binding domain (SBD) of Aspergillus flavus NSH9 was successfully identified, isolated, and overexpressed in Pichia pastoris GS115. The complete open reading frame of glucoamylase from Aspergillus flavus NSH9 was identified by employing PCR that encodes 493 amino acids lacking in the SBD. The first 17 amino acids were presumed to be a signal peptide. The cDNA was cloned into Pichia pastoris and the highest expression of recombinant glucoamylase (rGA) was observed after 8 days of incubation period with 1% methanol. The molecular weight of the purified rGA was about 78 kDa and exhibited optimum catalytic activity at pH 5.0 and temperature of 70°C. The enzyme was stable at higher temperature with 50% of residual activity observed after 20 min at 90°C and 100°C. Low concentration of metal (Mg(++), Fe(++), Zn(++), Cu(++), and Pb(++)) had positive effect on rGA activity. This rGA has the potential for use and application in the saccharification steps, due to its thermostability, in the starch processing industries.