Immobilized lysozyme protein on fibrous medium: Preliminary results for microfiltration applications
The protein lysozyme was deposited onto a permeable support comprising chemically functionalized glass fiber. The main objective of this study was to set a stable organic net with no effect on the medium bed permeability and a preliminary test the activity of this enzyme under immobilized conditions...
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Pontificia Universidad Católica de Valparaíso
2003
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oai:scielo:S0717-345820030002000102004-05-13Immobilized lysozyme protein on fibrous medium: Preliminary results for microfiltration applicationsAssis,Odilio B. G.Claro,Luis C The protein lysozyme was deposited onto a permeable support comprising chemically functionalized glass fiber. The main objective of this study was to set a stable organic net with no effect on the medium bed permeability and a preliminary test the activity of this enzyme under immobilized conditions. The film formation is followed by atomic force microscopy (AFM) surface imaging. The effect on the bacteria Escherichia coli was tested using a simple microfiltration column. The filtration results pointed around 75% removal of bacteria in the effluent when compared to the influent concentration. The removal mechanism is assumed as being essentially due biointeraction. The surface polarity characteristics of the formed film were also considered as playing an important role, suggesting an electrostatic interaction mechanism in the microorganism removal.info:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.6 n.2 20032003-08-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582003000200010es |
institution |
Scielo Chile |
collection |
Scielo Chile |
language |
Spanish / Castilian |
description |
The protein lysozyme was deposited onto a permeable support comprising chemically functionalized glass fiber. The main objective of this study was to set a stable organic net with no effect on the medium bed permeability and a preliminary test the activity of this enzyme under immobilized conditions. The film formation is followed by atomic force microscopy (AFM) surface imaging. The effect on the bacteria Escherichia coli was tested using a simple microfiltration column. The filtration results pointed around 75% removal of bacteria in the effluent when compared to the influent concentration. The removal mechanism is assumed as being essentially due biointeraction. The surface polarity characteristics of the formed film were also considered as playing an important role, suggesting an electrostatic interaction mechanism in the microorganism removal. |
author |
Assis,Odilio B. G. Claro,Luis C |
spellingShingle |
Assis,Odilio B. G. Claro,Luis C Immobilized lysozyme protein on fibrous medium: Preliminary results for microfiltration applications |
author_facet |
Assis,Odilio B. G. Claro,Luis C |
author_sort |
Assis,Odilio B. G. |
title |
Immobilized lysozyme protein on fibrous medium: Preliminary results for microfiltration applications |
title_short |
Immobilized lysozyme protein on fibrous medium: Preliminary results for microfiltration applications |
title_full |
Immobilized lysozyme protein on fibrous medium: Preliminary results for microfiltration applications |
title_fullStr |
Immobilized lysozyme protein on fibrous medium: Preliminary results for microfiltration applications |
title_full_unstemmed |
Immobilized lysozyme protein on fibrous medium: Preliminary results for microfiltration applications |
title_sort |
immobilized lysozyme protein on fibrous medium: preliminary results for microfiltration applications |
publisher |
Pontificia Universidad Católica de Valparaíso |
publishDate |
2003 |
url |
http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582003000200010 |
work_keys_str_mv |
AT assisodiliobg immobilizedlysozymeproteinonfibrousmediumpreliminaryresultsformicrofiltrationapplications AT claroluisc immobilizedlysozymeproteinonfibrousmediumpreliminaryresultsformicrofiltrationapplications |
_version_ |
1718441714564202496 |