Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 8635-8644 |
| Journal | Industrial and engineering chemistry research |
| Volume | 52 |
| Issue number | 26 |
| DOIs | |
| Publication status | Published - 2013 |
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Keywords
- METIS-297014
- IR-86783
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Enzymatic conversion in ion-exchange mixed matrix hollow fiber membranes. / Andre, Joao; Borneman, Zandrie; Wessling, Matthias.
In: Industrial and engineering chemistry research, Vol. 52, No. 26, 2013, p. 8635-8644.Research output: Contribution to journal › Article › Academic › peer-review
TY - JOUR
T1 - Enzymatic conversion in ion-exchange mixed matrix hollow fiber membranes
AU - Andre, Joao
AU - Borneman, Zandrie
AU - Wessling, Matthias
PY - 2013
Y1 - 2013
N2 - This work reports the adsorption of glucose oxidase (GOx) in particle-loaded hollow fibers using polyethersulfone as the matrix and Lewatit strong cation-exchange resins as the functional support. The activity of adsorbed GOx was evaluated under the same pH conditions as the adsorption. Static enzyme immobilization tests yielded high adsorption values at pHs below the isoelectric point (pI) of GOx, where the enzyme assumes the cationic form and adsorbs via electrostatic interaction. The adsorption by electrostatic interactions could be described by a Langmuir isotherm at pH values below the pI of GOx. Adsorption performed above the pI takes place preferentially via hydrophobic interactions. Dynamic GOx adsorption experiments resulted in the same values as those obtained in static experiments. Below the pI of the enzyme, the adsorption was found to be pH dependent. Above the pI of GOx, the adsorption was lower and independent of the pH. Formation of GOx multilayers was observed for all applied pH values. Dynamic glucose conversion measurements showed that the immobilized GOx retains an appreciable activity after adsorption via both methods. GOx immobilized via hydrophobic interactions yielded the highest activity values. Enzymes immobilized via electrostatic interaction showed multilayer adsorption, resulting in a strongly reduced enzymatic activity. The highest enzymatic activity of the adsorbed GOx was found for pH 5.0.
AB - This work reports the adsorption of glucose oxidase (GOx) in particle-loaded hollow fibers using polyethersulfone as the matrix and Lewatit strong cation-exchange resins as the functional support. The activity of adsorbed GOx was evaluated under the same pH conditions as the adsorption. Static enzyme immobilization tests yielded high adsorption values at pHs below the isoelectric point (pI) of GOx, where the enzyme assumes the cationic form and adsorbs via electrostatic interaction. The adsorption by electrostatic interactions could be described by a Langmuir isotherm at pH values below the pI of GOx. Adsorption performed above the pI takes place preferentially via hydrophobic interactions. Dynamic GOx adsorption experiments resulted in the same values as those obtained in static experiments. Below the pI of the enzyme, the adsorption was found to be pH dependent. Above the pI of GOx, the adsorption was lower and independent of the pH. Formation of GOx multilayers was observed for all applied pH values. Dynamic glucose conversion measurements showed that the immobilized GOx retains an appreciable activity after adsorption via both methods. GOx immobilized via hydrophobic interactions yielded the highest activity values. Enzymes immobilized via electrostatic interaction showed multilayer adsorption, resulting in a strongly reduced enzymatic activity. The highest enzymatic activity of the adsorbed GOx was found for pH 5.0.
KW - METIS-297014
KW - IR-86783
U2 - 10.1021/ie3028608
DO - 10.1021/ie3028608
M3 - Article
VL - 52
SP - 8635
EP - 8644
JO - Industrial and engineering chemistry research
JF - Industrial and engineering chemistry research
SN - 0888-5885
IS - 26
ER -