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Immobilization of myoglobin from horse skeletal muscle in hydrophilic polymer networks
Author(s) -
CastroForero Angelines,
Jiménez David,
LópezGarriga Juan,
TorresLugo Madeline
Publication year - 2007
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.26289
Subject(s) - self healing hydrogels , myoglobin , polymer chemistry , ethylene glycol , chemistry , methacrylate , polymer , polymerization , methacrylic acid , chemical engineering , materials science , organic chemistry , engineering
This work examines the immobilization of myoglobin from horse skeletal muscle in hydrophilic polymer networks. Due to specific changes in the spectroscopic properties of hemoproteins during ligand binding, they could be employed in optical sensing devices. Two immobilization techniques were considered: imbibition and entrapment. Anionic hydrogels composed of methacrylic acid (MAA), cationic hydrogels composed of dimethylamino ethyl methacrylate (DMAEM), and neutral hydrogels composed of poly(ethylene glycol) monomethyl ether monomethacrylate (PEGMA; molecular weight = 200, 400, or 1000), all crosslinked with poly(ethylene glycol) dimethacrylate (PEGDMA) (molecular weight = 200, 600, or 1000), were synthesized by free‐radical solution polymerization. By the imbibition method, MAA‐based hydrogels incorporated the highest amount of myoglobin in comparison with PEGMA or DMAEM polymers. The evaluation of the correlation length of the networks revealed that MAA hydrogels had the highest correlation length in comparison with PEGMA‐containing matrices or DMAEM hydrogels. Release experiments from MAA hydrogels at pHs 5.8 and 7.0 showed that the solute‐transport mechanism was a combination of Fickian and chain relaxation diffusion. Myoglobin‐loaded MAA hydrogels retained their heme reactivity after the immobilization process. The release of myoglobin incorporated by entrapment in MAA–PEGDMA hydrogels was highly influenced by the chain relaxation process. The diffusion coefficients of myoglobin incorporated by entrapment into anionic hydrogels were 2 orders of magnitude smaller (∼ 10–13) than those for myoglobin incorporated by imbibition (10–11), both evaluated at pH 7.0. Substrate binding studies indicated that the protein biological activity was not compromised in those hydrogels loaded by the imbibition method, whereas prepolymeric solutions showed detrimental effects on protein stability. © 2007 Wiley Periodicals, Inc. J Appl Polym Sci 2008