Immobilized carbonic anhydrase on hollow fiber membranes accelerates CO2 removal from blood

► CA-immobilization on hollow fiber membranes (HFMs). ► CA-HFMs increased CO2 removal efficiency from blood by 36%. ► CA-HFMs had 95% less platelet deposition. Current artificial lungs and respiratory assist devices designed for carbon dioxide removal (CO2R) are limited in their efficiency due to th...

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Bibliographic Details
Published in:Journal of membrane science 2012-06, Vol.403-404, p.25-31
Main Authors: Arazawa, David T., Oh, Heung-Il, Ye, Sang-Ho, Johnson, Carl A., Woolley, Joshua R., Wagner, William R., Federspiel, William J.
Format: Article
Language:English
Subjects:
Artificial lung
artificial membranes
bicarbonates
bioactive properties
blood
blood flow
carbon dioxide
carbonate dehydratase
Carbonic anhydrase
Chemistry
CO2 removal
Colloidal state and disperse state
enzyme activity
esterases
Exact sciences and technology
gas exchange
General and physical chemistry
Hollow fiber membrane
immobilized enzymes
lactate dehydrogenase
lungs
Membranes
radio waves
scanning electron microscopy
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Summary:► CA-immobilization on hollow fiber membranes (HFMs). ► CA-HFMs increased CO2 removal efficiency from blood by 36%. ► CA-HFMs had 95% less platelet deposition. Current artificial lungs and respiratory assist devices designed for carbon dioxide removal (CO2R) are limited in their efficiency due to the relatively small partial pressure difference across gas exchange membranes. To offset this underlying diffusional challenge, bioactive hollow fiber membranes (HFMs) increase the carbon dioxide diffusional gradient through the immobilized enzyme carbonic anhydrase (CA), which converts bicarbonate to CO2 directly at the HFM surface. In this study, we tested the impact of CA-immobilization on HFM CO2 removal efficiency and thromboresistance in blood. Fiber surface modification with radio frequency glow discharge (RFGD) introduced hydroxyl groups, which were activated by 1M CNBr while 1.5M TEA was added drop wise over the activation time course, then incubation with a CA solution covalently linked the enzyme to the surface. The bioactive HFMs were then potted in a model gas exchange device (0.0084m2) and tested in a recirculation loop with a CO2 inlet of 50mmHg under steady blood flow. Using an esterase activity assay, CNBr chemistry with TEA resulted in 0.99U of enzyme activity, a 3.3 fold increase in immobilized CA activity compared to our previous method. These bioactive HFMs demonstrated 108mL/min/m2 CO2 removal rate, marking a 36% increase compared to unmodified HFMs (p
ISSN:0376-7388
1873-3123
DOI:10.1016/j.memsci.2012.02.006