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Immobilization and stabilization of invertase using specific polyclonal antibodies
Author(s) -
Jafri F.,
Husain S.,
Saleemuddin M.
Publication year - 1993
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1993.tb00280.x
Subject(s) - invertase , antiserum , polyclonal antibodies , glutaraldehyde , enzyme , biochemistry , chemistry , sepharose , yeast , immobilized enzyme , specific activity , antibody , in vitro , chromatography , biology , immunology
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.