TY - JOUR
T1 - Functionalization of multiwalled carbon nanotubes by microwave irradiation for lysozyme attachment
T2 - Comparison of covalent and adsorption methods by kinetics of thermal inactivation
AU - Puentes-Camacho, Daniel
AU - Velázquez, Enrique F.
AU - Rodríguez-Félix, Dora E.
AU - Castillo-Ortega, Mónica
AU - Sotelo-Mundo, Rogerio R.
AU - Del Castillo-Castro, Teresa
N1 - Publisher Copyright:
© 2017 Vietnam Academy of Science & Technology.
PY - 2017/12
Y1 - 2017/12
N2 - Proteins suffer changes in their tertiary structure when they are immobilized, and enzymatic activity is affected due to the low biocompatibility of some supporting materials. In this work immobilization of lysozyme on carbon nanotubes previously functionalized by microwave irradiation was studied. The effectiveness of the microwave-Assisted acid treatment of carbon nanotubes was evaluated by XPS, TEM, Raman and FTIR spectroscopy. The carboxylic modification of nanotube surfaces by this fast, simple and feasible method allowed the physical adsorption and covalent linking of active lysozyme onto the carbonaceous material. Thermal inactivation kinetics, thermodynamic parameters and storage stability were studied for adsorbed and covalent enzyme complexes. A major stability was found for lysozyme immobilized by the covalent method, the activation energy for inactivation of the enzyme was higher for the covalent method and it was stable after 50 d of storage at 4 °C. The current study highlights the effect of protein immobilization method on the biotechnological potential of nanostructured biocatalysts.
AB - Proteins suffer changes in their tertiary structure when they are immobilized, and enzymatic activity is affected due to the low biocompatibility of some supporting materials. In this work immobilization of lysozyme on carbon nanotubes previously functionalized by microwave irradiation was studied. The effectiveness of the microwave-Assisted acid treatment of carbon nanotubes was evaluated by XPS, TEM, Raman and FTIR spectroscopy. The carboxylic modification of nanotube surfaces by this fast, simple and feasible method allowed the physical adsorption and covalent linking of active lysozyme onto the carbonaceous material. Thermal inactivation kinetics, thermodynamic parameters and storage stability were studied for adsorbed and covalent enzyme complexes. A major stability was found for lysozyme immobilized by the covalent method, the activation energy for inactivation of the enzyme was higher for the covalent method and it was stable after 50 d of storage at 4 °C. The current study highlights the effect of protein immobilization method on the biotechnological potential of nanostructured biocatalysts.
KW - carbon nanotubes
KW - kinetics
KW - lysozyme
KW - microwave irradiation
KW - thermal inactivation
UR - http://www.scopus.com/inward/record.url?scp=85039066609&partnerID=8YFLogxK
U2 - 10.1088/2043-6254/aa8b3c
DO - 10.1088/2043-6254/aa8b3c
M3 - Artículo
SN - 2043-6262
VL - 8
JO - Advances in Natural Sciences: Nanoscience and Nanotechnology
JF - Advances in Natural Sciences: Nanoscience and Nanotechnology
IS - 4
M1 - 045011
ER -