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Antimicrobial activity of glucose oxidase‐immobilized plasma‐activated polypropylene films
Author(s) -
Vartiainen Jari,
Rättö Marjaana,
Paulussen Sabine
Publication year - 2005
Publication title -
packaging technology and science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.365
H-Index - 50
eISSN - 1099-1522
pISSN - 0894-3214
DOI - 10.1002/pts.695
Subject(s) - glutaraldehyde , glucose oxidase , carbodiimide , covalent bond , immobilized enzyme , chemistry , bacillus subtilis , nuclear chemistry , polypropylene , polymer chemistry , enzyme , chromatography , organic chemistry , bacteria , biology , genetics
Antimicrobial enzyme, glucose oxidase (GOX), was covalently immobilized onto amino‐ and carboxyl‐plasma‐activated biorientated polypropylene films (BOPP) via glutaraldehyde and carbodiimide chemistries. N 2 ‐plasma + NH 3 and N 2 ‐plasma + CO 2 treatments were utilized to create amino (1.1 nmol/cm 2 ) and carboxyl (0.9 nmol/cm 2 ) groups densities onto the surface of BOPP films. GOX‐immobilized onto amino‐activated BOPP films using 2.5% glutaraldehyde produced higher enzymatic activities than GOX‐immobilized by 0.4% carbodiimide. Further immobilizations were carried out with glutaraldehyde as the coupling agent at temperatures of 4–75°C at pH 5.6 and 7.2. 10 s treatment was sufficient to immobilize GOX at high temperatures in both pH conditions, producing enzymatically active films which remained active over 30 days of storage. GOX covalently immobilized onto BOPP films completely inhibited the growth of Escherichia coli and substantially inhibited the growth of Bacillus subtilis ; thus, they may have great potential to be exploited in various antimicrobial packaging film applications. Copyright © 2005 John Wiley & Sons, Ltd.