Trypsin was immobilized onto a newly formulated nanocomposite (NC) comprising magnetic (Fe3O4) multiwalled carbon nanotubes (MWCNTs) anchored with polydopamine (PDA). The fabricated NC and the NC-bound trypsin were subjected to comprehensive characterization using various biophysical techniques including Fourier-transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), scanning electron microscopy (SEM), transmission electron microscopy (TEM), and fluorescence spectroscopy. The NC-bound trypsin exhibited significantly enhanced thermostability and increased tolerance to various organic solvents and denaturants. The enzymatic activity of trypsin was notably augmented through its coupling with the nano support, yielding an effectiveness factor (η) of 2.65. Fenugreek and ginger protein hydrolysates, prepared using both native and NC-bound enzyme, were evaluated for their antimicrobial activities. The analysis revealed that peptides generated by NC-bound trypsin showed higher antimicrobial activity (~ 10) in most cases compared to peptides obtained by using native trypsin. This strategy presents an innovative methodology for the production of potential biopeptides, with the prospect of their incorporation into pharmaceutical and therapeutic sectors through the utilization of NC-bound trypsin in protein hydrolysis.
Keywords: Antimicrobial activity; Biopeptide; Denaturants; Magnetic carbon nanotubes; Nanocomposite.
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