Immobilization of enzymes by bioaffinity layering.
Bioaffinity immobilization exploits the affinity of the enzyme to a macro-(affinity ligand). Such a macro-(affinity ligand) could be a lectin, a water-soluble polymer, or a bioconjugate of a water-soluble polymer and the appropriate affinity ligand. Successive layering of the enzyme and the macro-(affinity ligand) on a matrix allows deposition of a large amount of enzyme activity on a small surface. Illustrative protocols show affinity layering of a pectinase and horseradish peroxidase on Concanavalin A-agarose and Concanavalin A-Sephadex matrices, respectively.
Department of Chemistry, Indian Institute of Technology Delhi, New Delhi, India.
Veena
V
Singh
Meryam
M
Sardar
Munishwar Nath
MN
Gupta
D057075:Enzyme Assays; D004800:Enzymes, Immobilized / Q000737:chemistry*; D006735:Horseradish Peroxidase / Q000737:chemistry; D018551:Solanum lycopersicum / Q000201:enzymology; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification; D011096:Polygalacturonase / Q000737:chemistry / Q000302:isolation & purification; D011485:Protein Binding; D012685:Sepharose / Q000031:analogs & derivatives* / Q000737:chemistry
D004800:Enzymes, Immobilized; D010940:Plant Proteins; C028326:concanavalin A-sepharose; D012685:Sepharose; D006735:Horseradish Peroxidase; D011096:Polygalacturonase