Immobilization and stabilization of invertase using specific polyclonal antibodies.
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.
Jafri
F
F
Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, India.
Husain
S
S
Saleemuddin
M
M
D000818:Animals; D003432:Cross-Linking Reagents; D004789:Enzyme Activation / Q000187:drug effects; D004795:Enzyme Stability; D004800:Enzymes, Immobilized; D005976:Glutaral / Q000737:chemistry; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000276:immunology / Q000378:metabolism*; D007106:Immune Sera / Q000494:pharmacology; D005779:Immunodiffusion; D011817:Rabbits; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D043324:beta-Fructofuranosidase
D003432:Cross-Linking Reagents; D004800:Enzymes, Immobilized; D007106:Immune Sera; D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase; D005976:Glutaral