4.7 Article

Chemical modification of poly(ethylene terephthalate) and immobilization of the selected enzymes on the modified film

Journal

APPLIED SURFACE SCIENCE
Volume 255, Issue 19, Pages 8293-8298

Publisher

ELSEVIER
DOI: 10.1016/j.apsusc.2009.05.126

Keywords

PET film; Aminolysis; Invertase; Tyrosinase; Laccase; Enzyme activity

Funding

  1. Polish State Committee for Scientific Research [3T09C038 28, 343 585]

Ask authors/readers for more resources

Poly(ethylene terephthalate) (PET)film was modified by reaction with hydrazine (HD), ethylenediamine (EDA), 1,2-diaminopropane (1,2-DAP) and 1,3-diaminopropane (1,3-DAP). The maximal amount of amine functionalities introduced in the chosen conditions on the surface was found as 0.07, 3.35, 0.76 and 1.99 nmol cm(-2) for HD, EDA, 1,2-DAP and 1,3-DAP respectively. During the modification process etching of the sample and an increase of stiffness takes place. FTIR-ATR spectra prove that the surface chemistry after modi. cation in amine solution is very complex. The lack of clear correlation between the surface tension and surface concentration of amine functionalities seems to confirm that. For immobilization purpose invertase, laccase and tyrosinase were used. The amount of covalently attached proteins at first increases with the increase of surface concentration of amine groups but after reaching a certain level of amine groups, decrease of the immobilization level was observed. All enzymes tested showed highest activity for a moderate level of aminolysis and this activity had the highest values for EDA-modified PET. (C) 2009 Elsevier B. V. All rights reserved.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.7
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available