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Activity and stability of trypsin immobilized on chitosan magnetic nanoparticles

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Document pages: 10 pages

Abstract: The aim of this study was to covalently immobilize chitosan magnetic nanoparticles( Fe3O4@CTS )A trypsin with good thermal stability and operational stability was developed. It was confirmed by Fourier transform infrared spectroscopy (FTIR), X-ray photoelectron spectroscopy (XPS), X-ray diffraction (XRD) and transmission electron microscopy (TEM) Fe3O4@CTS The nanoparticles were successfully prepared, which showed that the preparation was effective Fe3O4@CTS Nanoparticles have superparamagnetism, with an average size of about 17   nm. Then, trypsin was covalently immobilized at high loading (149.25 ) Fe3O4@CTS On nanoparticles   mg g). FTIR data showed that compared with free trypsin, trypsin had conformational changes, Michaelis constant () andmaximum hydrolysis reaction rate () showed that the trypsin immobilized on the Fe3O4 @CTS had a lower affinity for BAEE and lower activity compared with free trypsin. However, the immobilized trypsin showed higher activity than free trypsin at pH 6.0 and in alkaline conditions and retained more than 84 of its initial activity at 60°C after 8 h incubation. Its excellent performance across a broader pH range and high thermal stability, as well as its effective hydrolysis of bovine serum albumin (BSA) and its reusability, make it more attractive than free trypsin for application in protein digestion.

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