Bisepoxide Cross-Linked Enzyme Aggregates – New Immobilized Biocatalysts for Selective Biotransformations

Weiser, Diána and Varga, A. and Kovács, K. and Nagy, F. and Szilágyi, András Ferenc and Vértessy G., Beáta and Paizs, Cs. and Poppe, László (2014) Bisepoxide Cross-Linked Enzyme Aggregates – New Immobilized Biocatalysts for Selective Biotransformations. CHEMCATCHEM, 6 (5). pp. 1463-1469. ISSN 1867-3880

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Abstract

Glycerol diglycidyl ether (GDE) is a convenient and inexpensive bis-epoxide cross-linker as demonstrated by the preparation of cross-linked enzyme aggregates (CLEAs) from two different enzyme classes. GDE cross-linked CLEAs of lipases from Pseudomonas fluorescens (AK), Burkholderia cepacia (PS) and lipase B from Candida antarctica (CaL B) and further of phenylalanine ammonia-lyase (PAL) from Petroselinum crispum showed improved properties as compared to their glutaraldehyde (GA) cross-linked counterparts. Ultrasonication studies indicated GDE cross-linked CLEAs of lipase PS and PAL as mechanically more stable than the GA-based forms. In the kinetic resolution of racemic 1-phenylethanol 1 catalytic activity of GDE-based 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 those of the corresponding GA-based lipase CLEAs (U= 24.4, 131.0 and 119.2 U g-1; for AK, CaL B and PS prepared at 22 °C, respectively). GDE-based PAL-bovine serum albumin co-CLEAs could be recycled at least three times when used for the stereoselective ammonia addition in 6M ammonia onto (E)-3-(thiophen-2-yl)acrylic acid 4 whereas recycling of conventional GA-based PAL CLEAs from this medium failed.

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