Immobilization of cross-linked lipase aggregates within microporous polymeric membranes

N. Hilal, R. Nigmatullin, A. Alpatova

Research output: Contribution to journalArticle

67 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)131-141
Number of pages11
JournalJournal of Membrane Science
Volume238
Issue number1-2
DOIs
Publication statusPublished - 15 Jul 2004
Externally publishedYes

Fingerprint

Polymeric membranes
Lipases
Lipase
immobilization
Immobilization
membranes
Membranes
enzymes
Enzymes
Hydrophobic and Hydrophilic Interactions
Hydrophobicity
hydrophobicity
1-Butanol
porosity
bioreactors
Oleic acid
Hydrophilicity
Polytetrafluoroethylene
Esterification
Hexanes

Keywords

  • Cross-linked enzyme aggregate
  • Esterifications
  • Lipase
  • Membrane bioreactor

ASJC Scopus subject areas

  • Filtration and Separation
  • Polymers and Plastics

Cite this

Immobilization of cross-linked lipase aggregates within microporous polymeric membranes. / Hilal, N.; Nigmatullin, R.; Alpatova, A.

In: Journal of Membrane Science, Vol. 238, No. 1-2, 15.07.2004, p. 131-141.

Research output: Contribution to journalArticle

Hilal, N. ; Nigmatullin, R. ; Alpatova, A. / Immobilization of cross-linked lipase aggregates within microporous polymeric membranes. In: Journal of Membrane Science. 2004 ; Vol. 238, No. 1-2. pp. 131-141.
@article{46696bb24f0048df86bdfb6ff7c89d60,
title = "Immobilization of cross-linked lipase aggregates within microporous polymeric membranes",
abstract = "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.",
keywords = "Cross-linked enzyme aggregate, Esterifications, Lipase, Membrane bioreactor",
author = "N. Hilal and R. Nigmatullin and A. Alpatova",
year = "2004",
month = "7",
day = "15",
doi = "10.1016/j.memsci.2004.04.002",
language = "English",
volume = "238",
pages = "131--141",
journal = "Journal of Membrane Science",
issn = "0376-7388",
publisher = "Elsevier",
number = "1-2",

}

TY - JOUR

T1 - Immobilization of cross-linked lipase aggregates within microporous polymeric membranes

AU - Hilal, N.

AU - Nigmatullin, R.

AU - Alpatova, A.

PY - 2004/7/15

Y1 - 2004/7/15

N2 - 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.

AB - 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.

KW - Cross-linked enzyme aggregate

KW - Esterifications

KW - Lipase

KW - Membrane bioreactor

UR - http://www.scopus.com/inward/record.url?scp=2942517661&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=2942517661&partnerID=8YFLogxK

U2 - 10.1016/j.memsci.2004.04.002

DO - 10.1016/j.memsci.2004.04.002

M3 - Article

AN - SCOPUS:2942517661

VL - 238

SP - 131

EP - 141

JO - Journal of Membrane Science

JF - Journal of Membrane Science

SN - 0376-7388

IS - 1-2

ER -