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

• Main Authors: Weiser, Diána, Varga, A., Kovács, K., Nagy, F., Szilágyi, András Ferenc, Vértessy G., Beáta, Paizs, Cs., Poppe, László
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 2014
• Subjects: QD Chemistry / kémia; Antarc*; Antarctica
• Online Access: https://real.mtak.hu/19300/; https://real.mtak.hu/19300/1/Weiser_ChemCatChem_2014.pdf; http://onlinelibrary.wiley.com/doi/10.1002/cctc.201300806/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.