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Purification, partial biochemical characterization and immobilization of Vigna mungo α-galactosidase on magnetic chitosan nanoparticles
6th World Congress on Biotechnology
Ramadevi Mutra, Deepesh Panwar and Mukesh Kapoor
CSIR-Central Food Technological Research Institute, India
Posters-Accepted Abstracts: J Biotechnol Biomater
Abstract
α-galactosidase (α-D-galactoside galacto hydrolase, E.C. 3.2.1.22) catalyses the hydrolysis of α-1, 6-linked terminal galactose residues from oligosaccharides like melibiose, raffinose and stachyose as well as galactomannans, galactolipids and galactoproteins. α-galactosidase have plethora of applications in food & feed (improvement in nutritional value food/feed, gelling properties of gums & beet sugar crystallization), medicine (blood group transformation, treatment of Anderson-Fabry’s disease and xeno-rejection) and paper & pulp industry. In the present study, α-galactosidase from locally available variety of black gram (Vigna mungo) seeds was purified to homogeneity by using a combination of citric acid precipitation, ammonium sulphate precipitation (25-60% saturation), DEAE-Cellulose, CM-Sepharose followed by ConA Sepharose 4B chromatography with 39.1% yield and 1500-fold purification. The purified enzyme migrated as a single band (Mw≈40 kDa) on silver stained SDS-PAGE. Purified α-galactosidase showed high activity in a narrow range of pH 4-5 with maximal activity at pH 5. The enzyme had less than 20% of its activity at acidic pH (3) or alkaline pH (8). The optimum temperature of α-galactosidase was found to be 55o C. Most of the tested metal ions were found to reduce the activity of α-galactosidase by up to 29% at 1 mM concentration. However, Hg++ drastically inhibited enzyme activity. The purified α-galactosidase was immobilized on chitosan iron oxide nanoparticles (α-GAL-MNP) using glutaraldehyde (540 mM) as a cross linker with high immobilization efficiency (≈90%). The α-galactosidase loaded nanoparticles were further characterized by Scanning Electron Microscopy and Fourier Transform Infrared Spectroscopy. Further, cross-linked enzyme aggregates of crude α-galactosidase were made and also immobilized on chitosan iron oxide nanoparticles (α-GAL-CLEA-MNP). The α-GAL-MNP and α-GAL-CLEA-MNP showed good retention of activity after repeated usage.Biography
Email: mkapoor@cftri.res.in
