|Title:||1,3-£]-Glucanase from Vigna aconitifolia and its possible use in enzyme bioreactor fabrication||Authors:||Kestwal R.M.
|Keywords:||£]-Glucanase;Characterization;Immobilization;Purification;Vigna aconitifolia||Issue Date:||2011||Source:||International Journal of Biological Macromolecules||Journal Volume:||49||Journal Issue:||5||Start page/Pages:||894-899||Abstract:||
Endo-1,3(4)-£]-glucanase (EC 126.96.36.199) 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.
|Appears in Collections:||食品科技研究所|
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