TY - JOUR
T1 - Enzymatic activation of cellulose acetate membrane for reducing of protein fouling
AU - Koseoglu-Imer, Derya Y.
AU - Dizge, Nadir
AU - Koyuncu, Ismail
PY - 2012/4/1
Y1 - 2012/4/1
N2 - In this study, the surface of cellulose acetate (CA) ultrafiltration membrane was activated with serine protease (Savinase) enzyme to reduce protein fouling. Enzyme molecules were covalently immobilized with glutaraldehyde (cross-linking agent) onto the surface of CA membranes. The membrane activation was verified using filtration experiments and morphological analysis. Scanning electron microscopy (SEM) images and attenuated total reflectance Fourier transform infrared (ATR-FTIR) spectroscopy of the activated membrane when compared with raw membrane were confirmed that the enzyme was immobilized onto the membrane surface. The immobilization efficiencies changed from 13.2 to 41.2% according to the enzyme ratios from 2.5 to 10.0mg/mL. However, the permeability values decreased from 232±6 to 121±4L/m 2hbar with increasing enzyme concentration from 2.5 to 10.0mg/mL. In fouling experiments, bovine serum albumin (BSA) was used as the protein model solution and activated sludge was used as the model biological sludge. Enzyme-activated membranes exhibited good filtration performances and protein rejection efficiencies were compared with raw CA membrane. Also the relative flux reduction (RFR) ratios of membranes were calculated as 97% and 88% for raw CA and enzyme-activated membranes (5mg/mL savinase), respectively. The membrane activated with Savinase enzyme could be proposed as a surface treatment method before filtration to mitigate protein fouling.
AB - In this study, the surface of cellulose acetate (CA) ultrafiltration membrane was activated with serine protease (Savinase) enzyme to reduce protein fouling. Enzyme molecules were covalently immobilized with glutaraldehyde (cross-linking agent) onto the surface of CA membranes. The membrane activation was verified using filtration experiments and morphological analysis. Scanning electron microscopy (SEM) images and attenuated total reflectance Fourier transform infrared (ATR-FTIR) spectroscopy of the activated membrane when compared with raw membrane were confirmed that the enzyme was immobilized onto the membrane surface. The immobilization efficiencies changed from 13.2 to 41.2% according to the enzyme ratios from 2.5 to 10.0mg/mL. However, the permeability values decreased from 232±6 to 121±4L/m 2hbar with increasing enzyme concentration from 2.5 to 10.0mg/mL. In fouling experiments, bovine serum albumin (BSA) was used as the protein model solution and activated sludge was used as the model biological sludge. Enzyme-activated membranes exhibited good filtration performances and protein rejection efficiencies were compared with raw CA membrane. Also the relative flux reduction (RFR) ratios of membranes were calculated as 97% and 88% for raw CA and enzyme-activated membranes (5mg/mL savinase), respectively. The membrane activated with Savinase enzyme could be proposed as a surface treatment method before filtration to mitigate protein fouling.
KW - Cellulose acetate membrane
KW - Covalent immobilization
KW - Enzymatic surface activation
KW - Protein fouling
KW - Savinase enzyme
UR - http://www.scopus.com/inward/record.url?scp=84856083773&partnerID=8YFLogxK
U2 - 10.1016/j.colsurfb.2011.12.013
DO - 10.1016/j.colsurfb.2011.12.013
M3 - Article
C2 - 22218336
AN - SCOPUS:84856083773
SN - 0927-7765
VL - 92
SP - 334
EP - 339
JO - Colloids and Surfaces B: Biointerfaces
JF - Colloids and Surfaces B: Biointerfaces
ER -
