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Collagen‐enzyme complex membranes and their performance in biocatalytic modules
Author(s) -
Wang S. S.,
Vieth W. R.
Publication year - 1973
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260150108
Subject(s) - chemistry , immobilized enzyme , glucose oxidase , invertase , lysozyme , enzyme , membrane , glucose 6 phosphate isomerase , biocatalysis , choline oxidase , urease , penicillin amidase , chromatography , biochemistry , catalysis , reaction mechanism , acetylcholinesterase
Abstract Collagen was used as carrier for the immobilization of invertase, lysozyme, urease, glucose oxidase, penicillin amidase, and glucose isomerase. Immobilization was accomplished by either impregnation of a preswollen collagen membrane with enzyme solution or electrocodeposition of collagen and enzyme from a collagen dispersion containing dissolved enzyme. The collagen‐enzyme complexes prepared are in membrane form. Membranous collagen‐enzyme complexes were used to construct biocatalytic reactors such as the capillaric coil modular reactor. Such biocatalytic reactors were used in a recirculation system for the conversion of substrates. The biocatalytic reactors showed initial decreases of activity to stable limits which are maintained over a large number of reactor volume replacements. The stable limits correspond to approximately 35% of the initial activities for lysozyme and invertase, 25% for urease, 15% for glucose oxidase. The mechanism of complex formation between collagen and enzyme involves multiple salt linkages, hydrogen bonds, and van der Waals interactions. This protein‐protein interaction which leads to stable complexes by both impregnation and electrocodeposition processes is unique among the enzyme immobilization methods currently available.