Bisepoxide cross-linked enzyme aggregates - New immobilized biocatalysts for selective biotransformations

Diána Weiser, Andrea Varga, Klaudia Kovács, Flóra Nagy, A. Szilágyi, B. Vértessy, Csaba Paizs, L. Poppe

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

Glycerol diglycidyl ether (GDE) is a convenient and inexpensive bisepoxide cross-linker as demonstrated by the preparation of cross-linked enzyme aggregates (CLEAs) from two enzyme classes. The GDE CLEAs of lipase from Pseudomonas fluorescens (AK), lipase from Burkholderia cepacia (PS), and lipase B from Candida antarctica (CaL B) as well as of phenylalanine ammonia-lyase (PAL) from Petroselinum crispum demonstrated improved properties as compared with their glutaraldehyde (GA) cross-linked counterparts. Ultrasonication studies indicated that the GDE CLEAs of lipase PS and PAL were mechanically more stable than the GA CLEAs. In the kinetic resolution of rac-1-phenylethanol, the catalytic activity of the GDE-lipase CLEAs (U=69.6, 134.8, and 127.4 U g -1 for AK, CaL B, and PS prepared at 22 °C, respectively) surpassed that of the corresponding GA-lipase CLEAs (U=24.4, 131.0, and 119.2 U g-1 for AK, CaL B, and PS prepared at 22 °C, respectively). The GDE co-CLEAs from PAL and bovine serum albumin (BSA) could be recycled at least three times if used for the stereoselective ammonia addition in 6 M ammonia to (E)-3-(thiophen-2-yl)acrylic acid, whereas the recycling of the conventional GA-PAL CLEAs from this medium failed. The missing linker: Glycerol diglycidyl ether is applied as a cross-linker for cross-linked enzyme aggregates (CLEAs) of various enzymes such as lipases and phenylalanine ammonia lyases. The bisepoxide CLEAs prove to be efficient and robust biocatalysts surpassing the performance of the glutaraldehyde CLEAs.

Original languageEnglish
Pages (from-to)1463-1469
Number of pages7
JournalChemCatChem
Volume6
Issue number5
DOIs
Publication statusPublished - 2014

Fingerprint

Biocatalysts
enzymes
Enzymes
Lipases
Phenylalanine Ammonia-Lyase
glycerols
ammonia
Glycerol
Ammonia
phenylalanine
Lipase
Ether
Ethers
ethers
Glutaral
Biotransformation
Enzyme kinetics
pseudomonas
Candida
acrylic acid

Keywords

  • biotransformations
  • cross-linked enzyme aggregate
  • enzyme catalysis
  • immobilization
  • lipase
  • phenylalanine ammonia-lyase

ASJC Scopus subject areas

  • Inorganic Chemistry
  • Organic Chemistry
  • Physical and Theoretical Chemistry
  • Catalysis

Cite this

Bisepoxide cross-linked enzyme aggregates - New immobilized biocatalysts for selective biotransformations. / Weiser, Diána; Varga, Andrea; Kovács, Klaudia; Nagy, Flóra; Szilágyi, A.; Vértessy, B.; Paizs, Csaba; Poppe, L.

In: ChemCatChem, Vol. 6, No. 5, 2014, p. 1463-1469.

Research output: Contribution to journalArticle

Weiser, Diána ; Varga, Andrea ; Kovács, Klaudia ; Nagy, Flóra ; Szilágyi, A. ; Vértessy, B. ; Paizs, Csaba ; Poppe, L. / Bisepoxide cross-linked enzyme aggregates - New immobilized biocatalysts for selective biotransformations. In: ChemCatChem. 2014 ; Vol. 6, No. 5. pp. 1463-1469.
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AU - Weiser, Diána

AU - Varga, Andrea

AU - Kovács, Klaudia

AU - Nagy, Flóra

AU - Szilágyi, A.

AU - Vértessy, B.

AU - Paizs, Csaba

AU - Poppe, L.

PY - 2014

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N2 - Glycerol diglycidyl ether (GDE) is a convenient and inexpensive bisepoxide cross-linker as demonstrated by the preparation of cross-linked enzyme aggregates (CLEAs) from two enzyme classes. The GDE CLEAs of lipase from Pseudomonas fluorescens (AK), lipase from Burkholderia cepacia (PS), and lipase B from Candida antarctica (CaL B) as well as of phenylalanine ammonia-lyase (PAL) from Petroselinum crispum demonstrated improved properties as compared with their glutaraldehyde (GA) cross-linked counterparts. Ultrasonication studies indicated that the GDE CLEAs of lipase PS and PAL were mechanically more stable than the GA CLEAs. In the kinetic resolution of rac-1-phenylethanol, the catalytic activity of the GDE-lipase CLEAs (U=69.6, 134.8, and 127.4 U g -1 for AK, CaL B, and PS prepared at 22 °C, respectively) surpassed that of the corresponding GA-lipase CLEAs (U=24.4, 131.0, and 119.2 U g-1 for AK, CaL B, and PS prepared at 22 °C, respectively). The GDE co-CLEAs from PAL and bovine serum albumin (BSA) could be recycled at least three times if used for the stereoselective ammonia addition in 6 M ammonia to (E)-3-(thiophen-2-yl)acrylic acid, whereas the recycling of the conventional GA-PAL CLEAs from this medium failed. The missing linker: Glycerol diglycidyl ether is applied as a cross-linker for cross-linked enzyme aggregates (CLEAs) of various enzymes such as lipases and phenylalanine ammonia lyases. The bisepoxide CLEAs prove to be efficient and robust biocatalysts surpassing the performance of the glutaraldehyde CLEAs.

AB - Glycerol diglycidyl ether (GDE) is a convenient and inexpensive bisepoxide cross-linker as demonstrated by the preparation of cross-linked enzyme aggregates (CLEAs) from two enzyme classes. The GDE CLEAs of lipase from Pseudomonas fluorescens (AK), lipase from Burkholderia cepacia (PS), and lipase B from Candida antarctica (CaL B) as well as of phenylalanine ammonia-lyase (PAL) from Petroselinum crispum demonstrated improved properties as compared with their glutaraldehyde (GA) cross-linked counterparts. Ultrasonication studies indicated that the GDE CLEAs of lipase PS and PAL were mechanically more stable than the GA CLEAs. In the kinetic resolution of rac-1-phenylethanol, the catalytic activity of the GDE-lipase CLEAs (U=69.6, 134.8, and 127.4 U g -1 for AK, CaL B, and PS prepared at 22 °C, respectively) surpassed that of the corresponding GA-lipase CLEAs (U=24.4, 131.0, and 119.2 U g-1 for AK, CaL B, and PS prepared at 22 °C, respectively). The GDE co-CLEAs from PAL and bovine serum albumin (BSA) could be recycled at least three times if used for the stereoselective ammonia addition in 6 M ammonia to (E)-3-(thiophen-2-yl)acrylic acid, whereas the recycling of the conventional GA-PAL CLEAs from this medium failed. The missing linker: Glycerol diglycidyl ether is applied as a cross-linker for cross-linked enzyme aggregates (CLEAs) of various enzymes such as lipases and phenylalanine ammonia lyases. The bisepoxide CLEAs prove to be efficient and robust biocatalysts surpassing the performance of the glutaraldehyde CLEAs.

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KW - lipase

KW - phenylalanine ammonia-lyase

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