Literature DB >> 23011348

Polyaniline-assisted silver nanoparticles: a novel support for the immobilization of α-amylase.

Mohammad Jahir Khan1, Qayyum Husain, Sajid Ali Ansari.   

Abstract

The size distribution of nanomaterials and their similarity in size with enzyme molecules together with other advantageous properties such as thermal stability, high surface-to-volume ratio, and irradiation resistance have revolutionized nanobiocatalytic approaches in various areas of enzyme technology. In the present study, polyaniline-assisted Ag nanocomposites were synthesized using ammonium peroxydisulfate as oxidant. These nanocomposites were used as a support for the covalent conjugation of α-amylase, one of the important industrial enzymes. X-ray diffraction study showed that the crystalline nature of nanocomposites was increased in the presence of Ag nanoparticles. Thermogravimetric and differential thermal analysis revealed that the synthesized nanocomposites retained significantly very high thermal stability. Scanning electron micrograph showed that Ag nanoparticles were homogeneously dispersed in polyaniline film providing large surface area and microenvironment for enzyme loading. Fourier transform infrared spectroscopy confirmed the conjugation of α-amylase to the functionalized nanocomposites. The conjugated α-amylase exhibited better tolerance to variations in the medium pH and temperature compared with the native enzyme. Immobilized α-amylase hydrolyzes starch more efficiently as compared to the free enzyme in batch process.

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Year:  2012        PMID: 23011348     DOI: 10.1007/s00253-012-4384-6

Source DB:  PubMed          Journal:  Appl Microbiol Biotechnol        ISSN: 0175-7598            Impact factor:   4.813


  1 in total

1.  Chloride Activated Halophilic α-Amylase from Marinobacter sp. EMB8: Production Optimization and Nanoimmobilization for Efficient Starch Hydrolysis.

Authors:  Sumit Kumar; S K Khare
Journal:  Enzyme Res       Date:  2015-01-18
  1 in total

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