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Immobilization of β‐galactosidase onto polymeric supports
Author(s) -
Rejikumar S.,
Devi Surekha
Publication year - 1995
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/app.1995.070550605
Subject(s) - immobilized enzyme , chitosan , vinyl alcohol , michaelis–menten kinetics , chemistry , formaldehyde , salicylic acid , covalent bond , resorcinol , enzyme assay , enzyme , polymer chemistry , nuclear chemistry , chromatography , chemical engineering , organic chemistry , polymer , biochemistry , engineering
Poly(vinyl alcohol) cross‐linked with para ‐formaldehyde (PVA–F) and natural polysaccharide–chitosan in bead form and salicylic acid–resorcinol–formaldehyde polymeric resin (SRF) in powder form were used for immobilization of β‐galactosidase through covalent linkages. Various activation processes and conditions were optimized. Immobilized enzyme showed very good storage stability at room temperature. Durability of the enzyme was also improved on immobilization. On repeated use of enzyme immobilized on chitosan beads, no loss was observed in enzyme activity even after 10 batches. Michaelis constant K m and maximum reaction velocity V m were calculated for free and immobilized enzyme systems. Effect of pH and temperature on enzyme activity was estimated and energy of activation ( E a ) and inactivation constant ( K i ) for free and immobilized enzyme were calculated. © 1995 John Wiley & Sons, Inc.