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Immobilization of catalase by polyion complex
Author(s) -
Kohjiya Shinzo,
Maeda Kazuyuki,
Yamashita Shinzo
Publication year - 1991
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.1991.070431210
Subject(s) - catalase , chemistry , titration , acrylamide , polymer chemistry , thermal stability , polyelectrolyte , methacrylate , sodium , enzyme , nuclear chemistry , polymer , inorganic chemistry , organic chemistry , monomer
Catalase was immobilized in a polyion complex from poly(sodium 2‐acrylamide‐2‐methyl‐1‐propanesulfonate) and poly[2‐(trimethylammonioethyl) methacrylate chloride]. Polyion complex formation between the two polyions was found to proceed stoichiometrically by the turbidimetric titration. Immobilization of catalase was achieved by conducting the complexation in the presence of the enzyme, which was established to be incorporated in the polyion complex networks. The fixed catalase showed higher thermal stability than the original enzyme. Furthermore, the stability and the activity of the fixed catalase were improved by annexing inert components such as albumin, histone, or lecithin at the time of polyion complex formation.