Construction Of Novel Metal-organic Hybrid Nanomaterials And Their Applications

The biomolecules are less stable and nonreusable;therefore a hybrid composite was introduced which constructed with the combination of metal-organic material.The construction of metal-organic composite occurred by bridging the organic ligands with the metal ions has acquired a much scientific interest.However,the stable metal-organic nanocomposite relies on numerous factors which play a vital role such as types of bonds and bridging ligand,nature of the interaction between metal and ligand.The mechanism of nanohybrid material formation takes place by incorporation of an aromatic ring or C-C double/triple bonds of ligands with the biomolecules.Metal-organic composites have been reported to be used in the pharmaceutical industry,food industry,textile industry and in many more industrial applications.Apart from its vast applications,it is still a challenging task to achieve highly active and stable metal-organic hybrid nanocomposite with minimum production cost.This work is devoted to do research and construct novel metal-organic hybrid materials and to apply on different applications with enhanced efficiency,excellent stability and profound reusability.These are the main themes that have been studied in this thesis:1.Constructed multiple enzyme systems by co-immobilizing the Glucose oxidase and Horseradish peroxidase enzymes in the carrier composed of GMP and matrix of Cu2+ions.GOx&HRP@Cu/GMP revealed significant improvement in the activity,stability,and selectivity.The stability of GOx&HRP@Cu/GMP was observed 8.5 times increased at 90?,while 10 times greater at pH 3 compared to free enzyme.The retention stability was noted to be 8 fold higher after thirteen days of storage compared to the free enzyme while 90%relative activity was sustained after eight consecutive usage cycles.The co-immobilized enzymes revealed with highly excellent stability against protease enzymes and the solvents of organic nature.GOx&HRP@Cu/GMP was also observed with excellent selectivity to be used as a glucose biosensor.2.The nanocomposite of hybrid nanoflower was formed by immobilizing enzyme alcalase using calcium hydrogen phosphate as a carrier.The formed nanocomposite alcalase@CaHPO4 was applied to the soybean protein isolates.The hydrolysis activity of nanocomposite of alcalase@CaHPO4 was observed 1.57 fold higher compared to its counterpart free alcalase.The stability of alcalase nanoflower was observed prominent with retaining 90%relative activity after using 7 cycles and at 70? and pH 4 revealed 100%and 65%relative activity respectively.Further,the nanocomposite of alcalase retained 80%relative activity after 10 days of storage.Furthermore,hydrolysates of soy protein produced by alcalase nanocomposite possessed higher radical-scavenging,calcium-binding capacity and solubility compared to produced by the free alcalase.3.In this study,a nanocomposite hematin@Cu/GMP with an excellent binding affinity of porphyrin ring towards Cu2+and GMP was studied.The hematin@Cu/GMP revealed excellent bi-enzyme mimicking activity against different substrates with relatively better performance than laccase and horseradish peroxidase enzyme.The potential catalytic activity of hematin@Cu/GMP at high temperature and harsh chemical conditions were suggestive of its high catalytic nature.The hematin@Cu/GMP composites showed 60%retention activity after five times of reusability and excellent stability against inorganic radical including cations,anions,and in the presence of other organic solvents.