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Distribution of an enzyme in porous polymer beads
Author(s) -
Ampon Kamaruzaman
Publication year - 1992
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/jctb.280550213
Subject(s) - amberlite , adsorption , penetration (warfare) , immobilized enzyme , chromatography , trypsin , polymer , porosity , bead , chemistry , michaelis–menten kinetics , enzyme , enzyme assay , materials science , chemical engineering , organic chemistry , composite material , operations research , engineering
Trypsin has been immobilized by adsorption onto Amberlite XAD‐7 beads. The Michaelis constant ( K m ) of the enzyme was increased about sevenfold following the immobilization. Its rate of penetration into the porous beads was determined by staining the beads, which had been split, with naphthol blue black. The extent of diffusional rate limitation of immobilized trypsin was related to the penetration depth of the enzyme into the beads. This can be controlled by manipulating the conditions during the preparation of the immobilized enzyme.