1,3-£]-Glucanase from Vigna aconitifolia and its possible use in enzyme bioreactor fabrication
Journal
International Journal of Biological Macromolecules
Journal Volume
49
Journal Issue
5
Pages
894-899
Date Issued
2011
Author(s)
Abstract
Endo-1,3(4)-£]-glucanase (EC 3.2.1.6) from Vigna aconitifolia sprouts was purified to 14.5 fold by gel filtration and ion-exchange chromatography. The enzyme was found to be a glycoprotein, its activity was Ca 2+ dependent and specific for £]-1,3 linkages in different polysaccharides. The K m value of the enzyme was estimated to be 3.0mgml -1 for £]-d-glucan as substrate. Circular dichroism studies revealed 8% £\-helix, 48% £]-pleated and 44% random coil in its secondary structure. Purified £]-glucanase was then successfully co-immobilized with glucose oxidase in agarose-chitosan beads, showing better immobilization yield, operational range and stability as compared with the crude £]-glucanase beads. The immobilized £]-glucanase was successfully used for mini-bioreactor fabrication. ? 2011 Elsevier B.V.
Subjects
£]-Glucanase
Characterization
Immobilization
Purification
Vigna aconitifolia
SDGs
Type
journal article