TY - JOUR
T1 - Functionalized membranes by layer-by-layer assembly of polyelectrolytes and in situ polymerization of acrylic acid for applications in enzymatic catalysis
AU - Datta, Saurav
AU - Cecil, Caitlyn
AU - Bhattacharyya, D.
PY - 2008/7/16
Y1 - 2008/7/16
N2 - This research work was directed toward the development of highly active, stable, and reusable functionalized polymeric membrane domains for enzymatic catalysis. Functionalized membranes were created by two different approaches. In the first approach, which involved alternative attachment of cationic and anionic polyelectrolytes, functionalization was performed using a layer-by-layer (LBL) assembly technique within a nylon-based microfiltration (MF) membrane. In the second approach, a hydrophobic polyvinylidene fluoride (PVDF) MF membrane was functionalized by the in situ polymerization of acrylic acid. The enzyme, glucose oxidase (GOX), was then electrostatically immobilized inside the functionalized membrane domains to study the catalytic oxidation of glucose to gluconic acid and H2O2. Characterization of the functionalized membranes, in terms of polyelectrolyte/polymer domains and permeate flux, was also conducted. The kinetics of H2O2 formation was discussed, along with the effects of residence time and pH on the activity of GOX. The stability and reusability of the electrostatically immobilized enzymatic system were also investigated.
AB - This research work was directed toward the development of highly active, stable, and reusable functionalized polymeric membrane domains for enzymatic catalysis. Functionalized membranes were created by two different approaches. In the first approach, which involved alternative attachment of cationic and anionic polyelectrolytes, functionalization was performed using a layer-by-layer (LBL) assembly technique within a nylon-based microfiltration (MF) membrane. In the second approach, a hydrophobic polyvinylidene fluoride (PVDF) MF membrane was functionalized by the in situ polymerization of acrylic acid. The enzyme, glucose oxidase (GOX), was then electrostatically immobilized inside the functionalized membrane domains to study the catalytic oxidation of glucose to gluconic acid and H2O2. Characterization of the functionalized membranes, in terms of polyelectrolyte/polymer domains and permeate flux, was also conducted. The kinetics of H2O2 formation was discussed, along with the effects of residence time and pH on the activity of GOX. The stability and reusability of the electrostatically immobilized enzymatic system were also investigated.
UR - http://www.scopus.com/inward/record.url?scp=49149149668&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=49149149668&partnerID=8YFLogxK
U2 - 10.1021/ie800142d
DO - 10.1021/ie800142d
M3 - Article
AN - SCOPUS:49149149668
SN - 0888-5885
VL - 47
SP - 4586
EP - 4597
JO - Industrial and Engineering Chemistry Research
JF - Industrial and Engineering Chemistry Research
IS - 14
ER -