A. Ramankannan, J. Rini Gnana Suganthi, N.Balaji, M. Seenuvasan
A. Ramankannan1, J. Rini Gnana Suganthi1, N.Balaji2, M. Seenuvasan2*
1IV Year B.Tech-Biotechnology, Department of Biotechnology, Madha Engineering College, Chennai, India.
2Assistant Prof & Head, Department of Biotechnology, Madha Engineering College, Chennai, India.
Volume - 3,
Issue - 4,
Year - 2013
The binding of pectinase onto co-precipitated magnetic magnetic nanoparticles (MNPs) via glutaraldehyde activation was investigated.The transmission electron microscopy (TEM), X-ray diffraction (XRD) analysis and Fourier transform infrared (FT-IR) spectroscopy were studied to characterize size, structure, morphology and binding of enzyme onto the nanoparticles. Debye-Scherrer relation was analysed based on the XRD results, reports that binding process did not cause any significant change in size of MNPs. The maximum activity of immobilized pectinase was obtained at its weight ratio of about 16.2 x10-3 mg bound pectinase/mg MNPs. The stability and activity of the bound pectinase was analyzed using various parameters like pH, temperature, reusability, storage ability and kinetic studies. The same was compared with the free pectinase for showing its enhanced stability and activity.
Cite this article:
A. Ramankannan, J. Rini Gnana Suganthi, N.Balaji, M. Seenuvasan. Preparation and Characterization of Pectinase bound Co-precipitated Magnetic Nanoparticles . Asian J. Pharm. Tech. 2013; Vol. 3: Issue 4, Pg 175-180.