Author(s): Bonshikachatterjee, Nivetha. A, Mohanasrinivasan. V

Email(s): v.mohan@vit.ac.in

DOI: 10.5958/0974-360X.2018.00275.5   

Address: Bonshikachatterjee, Nivetha. A, Mohanasrinivasan. V
School of Bio Sciences and Technology, VIT University, Vellore, Tamil Nadu
*Corresponding Author

Published In:   Volume - 11,      Issue - 4,     Year - 2018


ABSTRACT:
The immobilization of lactase (ß-galactosidase) enzyme was achieved by entrapping it in chitosan-alginate composite scaffolds, which were formed by ionotropic pre-gelation followed by a pH increase to synthesize polyelectrolyte complex scaffolds, and subsequent cross-linking and activation by glutaraldehyde. The operational stability upon storage of the enzyme entrapped was checked by performing batch hydrolysis of lactose concentrations ranging from 1mg/ml to 5mg/ml and the resulting glucose produced in every reaction was determined using the glucose oxidase-peroxidase assay. This study also investigates the stability of the free and immobilized enzymes at altered sets of pH and temperature at a fixed concentration of enzyme for the reaction medium. Morphology and structure characterization of lyophilized composite scaffolds were examined using scanning electron microscope and Fourier transform infra-red spectra, respectively.


Cite this article:
Bonshikachatterjee, Nivetha. A, Mohanasrinivasan. V. Immobilization of β-galactosidase in Chitosan-Alginate composite scaffolds and optimization of lactose hydrolysis. Research J. Pharm. and Tech 2018; 11(4): 1480-1485. doi: 10.5958/0974-360X.2018.00275.5

Cite(Electronic):
Bonshikachatterjee, Nivetha. A, Mohanasrinivasan. V. Immobilization of β-galactosidase in Chitosan-Alginate composite scaffolds and optimization of lactose hydrolysis. Research J. Pharm. and Tech 2018; 11(4): 1480-1485. doi: 10.5958/0974-360X.2018.00275.5   Available on: https://rjptonline.org/AbstractView.aspx?PID=2018-11-4-39


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RNI: CHHENG00387/33/1/2008-TC                     
DOI: 10.5958/0974-360X 

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