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Surface functionalization of porous polypropylene membranes with polyaniline for protein immobilization
Author(s) -
Piletsky Sergey,
Piletska Elena,
Bossi Alessandra,
Turner Nicholas,
Turner Anthony
Publication year - 2003
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.10544
Subject(s) - membrane , polyaniline , ammonium persulfate , horseradish peroxidase , adsorption , immobilized enzyme , chemical engineering , chemistry , surface modification , polypropylene , polymerization , polymer chemistry , chromatography , polymer , organic chemistry , enzyme , biochemistry , engineering
Commercial porous polypropylene membranes were chemically modified with polyaniline (PANI) using ammonium persulfate as the oxidizer. The influence of polymerization conditions on the membrane properties was studied by adsorption analysis and membrane permeability. The PANI‐coated polypropylene (PANI/PP) membranes possessed high affinity toward the proteins, which can be immobilized onto the membrane surface through physical adsorption or covalent immobilization. The quantity of immobilized horseradish peroxidase (HRP) and its activity depended on the quantity and quality (oxidation level) of PANI. The storage conditions for PANI/PP membranes containing immobilized HRP were studied. HRP immobilized on the PANI/PP membrane was shown to retain 70% of its activity after 3‐month storage at +5°C, suggesting that this material can be used for practical application, such as in bioreactors as enzyme membranes. © 2003 Wiley Periodicals, Inc. Biotechnol Bioeng 82: 86–92, 2003.