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Immobilization and stabilization of invertase using specific polyclonal antibodies
F Jafri1, S Husain, M Saleemuddin
1Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, India.
Antisera raised in rabbits to baker's-yeast invertase significantly activated the enzyme in vitro. The antisera contained precipitating antibodies, a significant fraction of which appeared to be directed against the glycosyl residues of the enzyme. Invertase could be immobilized as insoluble enzyme antibody adducts or by binding to a Sepharose matrix precoupled with the gamma-globulin fraction derived from the antisera. The immobilized invertase preparations exhibited high enzyme activity and had markedly enhanced thermal stability, which could be further improved by cross-linking with glutaraldehyde.
Antisera raised in rabbits to baker's-yeast invertase significantly activated the enzyme in vitro. The antisera contained precipitating antibodies, a significant fraction of which appeared to be directed against the glycosyl residues of the enzyme. Invertase could be immobilized as insoluble enzyme antibody adducts or by binding to a Sepharose matrix precoupled with the gamma-globulin fraction derived from the antisera. The immobilized invertase preparations exhibited high enzyme activity and had markedly enhanced thermal stability, which could be further improved by cross-linking with glutaraldehyde.
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