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Immobilization of cross-linked lipase aggregates within microporous polymeric membranes

✍ Scribed by N Hilal; R Nigmatullin; A Alpatova


Publisher
Elsevier Science
Year
2004
Tongue
English
Weight
550 KB
Volume
238
Category
Article
ISSN
0376-7388

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✦ Synopsis


A new approach is proposed to immobilize lipase into microporous polymeric membrane via embedding cross-linked enzyme aggregates (CLEA) within membrane pores. Preparation of biocatalytic membranes was implemented with hydrophilic cellulose and hydrophobic PTFE membranes. Formation of lipase CLEAs is initiated by solvent exchange between aqueous solution of the enzyme filling membrane pores and organic media containing cross-linking agent. The influence of organic media composition and matrix hydrophilicity/hydrophobicity on membrane biocatalytic properties has been studied. Highly effective biocatalytic membranes with embedded lipase CLEA have been obtained on the base of both hydrophilic and hydrophobic membranes by varying the content of glutaric dialdehyde used as a cross-linking agent. Bio-imprinting has been tested as a mean to improve efficiency of the biocatalytic membranes. Biocatalytic esterification of oleic acid with n-butanol has been studied in cross-flow membrane bioreactor with membrane-supported lipase CLEA using hexane and iso-octane as reaction solvents of different hydrophobicity.


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Immobilization of cross-linked lipase ag
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## Abstract __Candida rugosa__ lipase was immobilized on amino‐functionalized magnetic supports via cross‐linked enzyme aggregates (CLEA) and used to enhance the enzymatic degradation of polycaprolactone (PCL). The maximum amounts of lipase immobilized on the magnetic beads using glutaraldehyde as