The immobilisation of proteases produced by SSF onto functionalized magnetic nanoparticles: Application in the hydrolysis of different protein sources

Publication date: Available online 16 January 2017 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Noraziah Abu Yazid, Raquel Barrena, Antoni Sánchez Alkaline proteases produced from protein-rich waste (hair waste and soya residues) by solid state fermentation (SSF) were immobilised onto functionalized magnetic iron oxide nanoparticles (MNPs) using glutaraldehyde as a crosslinking agent. The covalent binding method had a better immobilisation yield compared to simple adsorption, retaining 93%-96% (459±106U/mg nanoparticles, 319±34U/mg nanoparticles) of hair waste and soya residues proteases, respectively after crosslinking with 5% glutaraldehyde for 6h. However, the adsorption immobilisation yield was 47%-54% after 8h for both proteases. MNPs and immobilised proteases were characterized using transmission electron microscopy (TEM), scanning electron microscopy (SEM), Fourier transform infrared spectroscopy (FT-IR) and electron diffraction. Our results indicated successful crosslinking between the proteases and amino-functionalized MNPs. The operational stability (pH and temperature) and storage stability of free and immobilised enzyme were also analysed. Despite the fact that the optimum pH of free and immobilised proteases was identical in the alkaline region, the immobilised proteases reached their optimum condition at higher temperatures (40°C − 60°C). After 2 months of storage at 4°C, the immobilised proteases showed good stability, retaining mo...
Source: Journal of Molecular Catalysis B: Enzymatic - Category: Biochemistry Source Type: research