Antimicrobial activity of glucose oxidase-immobilized plasma-activated polypropylene films

Abstract

Antimicrobial enzyme, glucose oxidase (GOX), was covalently immobilized onto amino- and carboxyl-plasma-activated biorientated polypropylene films (BOPP) via glutaraldehyde and carbodiimide chemistries. N2-plasma + NH3 and N2-plasma + CO2 treatments were utilized to create amino (1.1 nmol/cm2) and carboxyl (0.9 nmol/cm2) 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.