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Your search keyword '"Nanoflowers And Nanofibers"' showing total 2 results
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2 results on '"Nanoflowers And Nanofibers"'

1. Peroxidase-like Catalytic Activity of Copper-Mediated Protein-Inorganic Hybrid Nanoflowers and Nanofibers of β-Lactoglobulin and α-Lactalbumin: Synthesis, Spectral Characterization, Microscopic Features, and Catalytic Activity

Author

Chebrolu P. Rao and Atul Gajanan Thawari

Subjects
Dimer, Metal-Ions, Inorganic chemistry, Nanofibers, Protein dimer, Nanoparticle, 02 engineering and technology, Lactoglobulins, 010402 general chemistry, 01 natural sciences, Fluorescence spectroscopy, Catalysis, chemistry.chemical_compound, Whey, General Materials Science, Protein secondary structure, Peroxidase Activity, Peroxidase, Gel electrophoresis, Nanobiomaterial, Nanoflowers And Nanofibers, Ph, Catalytic Activity, Nanoflower, Binding, 021001 nanoscience & nanotechnology, 0104 chemical sciences, Nanostructures, Zinc, chemistry, Peroxidases, Protein-Inorganic Hybrid, Peptide, Lactalbumin, Thermal Aggregation, Fibrils, 0210 nano-technology, Copper, Nuclear chemistry, Protein Dimer
Abstract

A free Cys-SH-containing protein, beta-lactoglobulin (beta-LG), and another protein not possessing the same, viz., apo-alpha-lactoglobulin (apo-alpha-LA), were used in studies to demonstrate the role of this amino acid, along with its secondary structure, in the formation of a protein dimer and a protein-inorganic hybrid nanoflower and in the creation of the peroxidase-like activity of the nanomaterials produced when the proteins were treated with varying Cu2+ concentration under different pH conditions. An increase in the pH as well as the Cu2+ mole ratio results in increasing dimer formation in case of beta-LG due to the presence of free Cys121-SH, while the dimer is not formed in case of apo-alpha-LA under the same conditions. The role of Cys in the dimer formation has been demonstrated both by MALDI and sodium dodecyl sulfate-polyacrylamide gel electrophoresis studies. Both of the proteins exhibited changes in their secondary structures to different extents as a function of pH, and the structures were stabilized by Cu2+ interactions, as studied by CD and fluorescence spectroscopy. The small and spherical nanoparticles formed at pH 7 with lower equivalents of Cu2+ join together to form larger aggregates at higher equivalents of Cu2+. For the same concentration at pH 9, both the aggregates and the nanoflowers were noticed. However, at pH 12, the Cu2+ binding induces the formation of fibers along with the flowers. Both the nanoflowers and nanofibers exhibited peroxidase-like activity in a catalytic manner. Nanoflowers were also shown to detect phenol in the concentration range from 10 to 200 mu M. The copper-induced nanobiomaterial obtained in the case of apo-alpha-LA also exhibited peroxidase-like activity. Thus, this paper deals with the green synthesis of copper-induced protein (beta-LG/apo-alpha-LA)-inorganic hybrid nanomaterials that are important due to their applications as nanobiomaterials.

Published
2016

2. Peroxidase-like Catalytic Activity of Copper-Mediated Protein-Inorganic Hybrid Nanoflowers and Nanofibers of β-Lactoglobulin and α-Lactalbumin: Synthesis, Spectral Characterization, Microscopic Features, and Catalytic Activity.

Author

Thawari AG and Rao CP

Subjects
Catalysis, Copper, Lactalbumin, Lactoglobulins, Nanofibers, Peroxidase, Peroxidases, Nanostructures
Abstract

A free Cys-SH-containing protein, β-lactoglobulin (β-LG), and another protein not possessing the same, viz., apo-α-lactoglobulin (apo-α-LA), were used in studies to demonstrate the role of this amino acid, along with its secondary structure, in the formation of a protein dimer and a protein-inorganic hybrid nanoflower and in the creation of the peroxidase-like activity of the nanomaterials produced when the proteins were treated with varying Cu(2+) concentration under different pH conditions. An increase in the pH as well as the Cu(2+) mole ratio results in increasing dimer formation in case of β-LG due to the presence of free Cys121-SH, while the dimer is not formed in case of apo-α-LA under the same conditions. The role of Cys in the dimer formation has been demonstrated both by MALDI and sodium dodecyl sulfate-polyacrylamide gel electrophoresis studies. Both of the proteins exhibited changes in their secondary structures to different extents as a function of pH, and the structures were stabilized by Cu(2+) interactions, as studied by CD and fluorescence spectroscopy. The small and spherical nanoparticles formed at pH 7 with lower equivalents of Cu(2+) join together to form larger aggregates at higher equivalents of Cu(2+). For the same concentration at pH 9, both the aggregates and the nanoflowers were noticed. However, at pH 12, the Cu(2+) binding induces the formation of fibers along with the flowers. Both the nanoflowers and nanofibers exhibited peroxidase-like activity in a catalytic manner. Nanoflowers were also shown to detect phenol in the concentration range from 10 to 200 μM. The copper-induced nanobiomaterial obtained in the case of apo-α-LA also exhibited peroxidase-like activity. Thus, this paper deals with the green synthesis of copper-induced protein (β-LG/apo-α-LA)-inorganic hybrid nanomaterials that are important due to their applications as nanobiomaterials.

Published
2016
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