TY - JOUR
T1 - Immobilization of cellulase on functionalized cobalt ferrite nanoparticles
AU - Bohara, Raghvendra Ashok
AU - Thorat, Nanasaheb Devappa
AU - Pawar, Shivaji Hariba
N1 - Publisher Copyright:
© 2016, Korean Institute of Chemical Engineers, Seoul, Korea.
PY - 2016/1/1
Y1 - 2016/1/1
N2 - Amine functionalized cobalt ferrite (AF-CoFe2O4) magnetic nanoparticles (MNPs) were used for immobilization of cellulase enzyme via 1-ethyl-3-[3-dimethylaminopropyl] carbodiimide hydrochloride (EDS) and N-hydroxy-succinimide (NHS) coupling reaction. The structural, morphological and magnetic properties of AF-CoFe2O4 were determined. TEM micrograph revealed a mean diameter of ∼8 nm and showed that the AF-CoFe2O4 remain distinct with no significant change in size after binding with cellulase. Fourier transform infrared (FT-IR) spectroscopy confirmed the binding of cellulase to AF-CoFe2O4. The properties of immobilized cellulase were investigated by optimizing binding efficiency, pH, temperature and reusability. The results showed that the immobilized cellulase has higher thermal stability than free cellulase, which might be due to covalent interaction between cellulase and AF-CoFe2O4 surface. The immobilized cellulase also showed good reusability after recovery. Therefore, AF-CoFe2O4 MNPs can be considered as promising candidate for enzyme immobilization.
AB - Amine functionalized cobalt ferrite (AF-CoFe2O4) magnetic nanoparticles (MNPs) were used for immobilization of cellulase enzyme via 1-ethyl-3-[3-dimethylaminopropyl] carbodiimide hydrochloride (EDS) and N-hydroxy-succinimide (NHS) coupling reaction. The structural, morphological and magnetic properties of AF-CoFe2O4 were determined. TEM micrograph revealed a mean diameter of ∼8 nm and showed that the AF-CoFe2O4 remain distinct with no significant change in size after binding with cellulase. Fourier transform infrared (FT-IR) spectroscopy confirmed the binding of cellulase to AF-CoFe2O4. The properties of immobilized cellulase were investigated by optimizing binding efficiency, pH, temperature and reusability. The results showed that the immobilized cellulase has higher thermal stability than free cellulase, which might be due to covalent interaction between cellulase and AF-CoFe2O4 surface. The immobilized cellulase also showed good reusability after recovery. Therefore, AF-CoFe2O4 MNPs can be considered as promising candidate for enzyme immobilization.
KW - Bio-catalysis
KW - Cellulase
KW - Cobalt Ferrite
KW - Immobilization
KW - Superparamagnetic Nanoparticles
UR - http://www.scopus.com/inward/record.url?scp=84952628167&partnerID=8YFLogxK
U2 - 10.1007/s11814-015-0120-0
DO - 10.1007/s11814-015-0120-0
M3 - Article
AN - SCOPUS:84952628167
SN - 0256-1115
VL - 33
SP - 216
EP - 222
JO - Korean Journal of Chemical Engineering
JF - Korean Journal of Chemical Engineering
IS - 1
ER -