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Preparation of regenerable magnetic nanoparticles for cellulase immobilization: Improvement of enzymatic activity and stability
Author(s) -
Ozyilmaz Elif,
Alhiali Ahmet,
Caglar Ozge,
Yilmaz Mustafa
Publication year - 2021
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1002/btpr.3145
Subject(s) - cellulase , thermogravimetric analysis , nuclear chemistry , chemistry , magnetic nanoparticles , hydrolysis , nanoparticle , superparamagnetism , silane , glutaraldehyde , fourier transform infrared spectroscopy , copper , chromatography , materials science , chemical engineering , organic chemistry , nanotechnology , physics , magnetization , quantum mechanics , magnetic field , engineering
To obtain regenerable magnetic nanoparticles, triethoxy(3‐isocyanatopropyl)silane and iminodiacetic acid (IZ) were used as the starting material and immobilized on Fe 3 O 4 nanoparticles. Copper ions (Cu 2+ ions) were loaded on the Fe‐IZ nanoparticles and used for cellulase immobilization. The support was characterized by spectroscopic methods (FTIR, NMR) and thermogravimetric analysis, transmission electron microscopy, scanning electron microscope, X‐ray diffraction, energy dispersive X‐ray analysis, and vibrating sample magnetometer techniques. As a result of experiments, the amount of protein bound to immobilized cellulase (Fe‐IZ‐Cu‐E) and cellulase activity was found to be 33.1 mg/g and 154 U/g at pH 5, 50°C, for 3 h. The results indicated that the free cellulase had kept only 50% of its activity after 2 h, while the Fe‐IZ‐Cu‐E was observed to be around 77%, at 60°C. It was found that the immobilized cellulase maintained 93% of its initial catalytic activity after its sixth use. Furthermore, the Fe‐IZ‐Cu‐E retained about 75% of its initial activity after 28 days of storage. To reuse the support material (Fe‐IZ‐Cu), it was regenerated by thorough washing with ammonia or imidazole.