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Prof. Sivanesan Subramanian

Anna University, India

 

Prof. Hassan Karimi-Maleh

University of Electronic Science
and Technology of China (UESTC)

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Home > Archives > Vol 7, No 2 (Published) > Original Research Article
ACE-2064

Published

2024-04-15

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Vol 7, No 2 (Published)

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Original Research Article

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Copyright (c) 2024 yilmaz yurekli, Sadika Guedidi Bernard, Sacide Alsoy Altinkaya, André Deratani, Christophe Innocent

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How to Cite

Yurekli, Y., Guedidi, S., Altinkaya, S. A., Deratani, A., & Innocent, C. (2024). Behavior of enzymatic membranes under pressure: Effect of enzyme location. Applied Chemical Engineering, 7(2), 2064. https://doi.org/10.59429/ace.v7i2.2064
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Behavior of enzymatic membranes under pressure: Effect of enzyme location

Yilmaz Yurekli

Bioengineering Department, Manisa Celal Bayar University

Sadika Guedidi

European Membrane Institute, Montpellier 2 University (ENSCM, UM2, CNRS)

Sacide Alsoy Altinkaya

Department of Chemical Engineering, Izmir Institute of Technology

André Deratani

European Membrane Institute, Montpellier 2 University (ENSCM, UM2, CNRS)

Christophe Innocent

European Membrane Institute, Montpellier 2 University (ENSCM, UM2, CNRS)


DOI: https://doi.org/10.59429/ace.v7i2.2064


Keywords: enzymatic membrane; LbL self assembly; mass transfer resistance; long term stability; trypsin; urease


Abstract

Enzyme immobilized membranes combine catalysis and separation functions. Their application in large-scale continuous processes requires knowing the behavior under pressure. Also, the effects of enzyme location on the mass transfer limitation, membranes’ stability, and filtration performance should be investigated. In this study, urease (URE) and trypsin (TRY) enzymes were physically immobilized in/on the surface of a polyacrylonitrile (AN69) membrane through layer-by-layer (LbL) self-assembly method using polyethylenemine (PEI) and sodium-alginate (ALG) as cationic and anionic polyelectrolytes respectively. URE, located on the membrane’s surface, degraded urea in a reaction-controlled regime, and its immobilization did not significantly change the hydraulic permeability. On the other hand, the TRY enzyme attached to the membrane’s pores reduced the permeability and degraded the BAPNA in a diffusion-controlled region. In TRY immobilized membranes, the conversion increased linearly with the transmembrane pressure, while in URE immobilized ones, conversion was maximum at 1 bar. Sandwiching the enzymes between two polyelectrolytes resulted in the highest catalytic activities. This configuration maintained most of the URE activity in the long-term filtration, but it did not help prevent TRY’s activity loss.


Author Biographies

Yilmaz Yurekli, Bioengineering Department, Manisa Celal Bayar University

Bioengineering Department

Sadika Guedidi, European Membrane Institute, Montpellier 2 University (ENSCM, UM2, CNRS)

Institut Européen des Membranes

Sacide Alsoy Altinkaya, Department of Chemical Engineering, Izmir Institute of Technology

Chemical Engineering Department

André Deratani, European Membrane Institute, Montpellier 2 University (ENSCM, UM2, CNRS)

Institut Européen des Membranes

Christophe Innocent, European Membrane Institute, Montpellier 2 University (ENSCM, UM2, CNRS)

Institut Européen des Membranes


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