| Autor: |
Valerio Ferrario, Anamaria Todea, Lisa Wolansky, Nicola Piovesan, Alice Guarneri, Doris Ribitsch, Georg M. Guebitz, Lucia Gardossi, Alessandro Pellis |
| Jazyk: |
angličtina |
| Rok vydání: |
2022 |
| Předmět: |
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| Zdroj: |
Catalysts, Vol 12, Iss 3, p 303 (2022) |
| Druh dokumentu: |
article |
| ISSN: |
2073-4344 |
| DOI: |
10.3390/catal12030303 |
| Popis: |
In relation to the development of environmentally-friendly processing technologies for the continuously growing market of plastics, enzymes play an important role as green and sustainable biocatalysts. The present study reports the use of heterogeneous immobilized biocatalysts in solvent-free systems for the synthesis of aliphatic oligoesters with Mws and monomer conversions up to 1500 Da and 74%, respectively. To improve the accessibility of hydrophilic and hydrophobic substrates to the surface of the biocatalyst and improve the reaction kinetic and the chain elongation, two different binding modules were fused on the surface of cutinase 1 from Thermobifida cellulosilytica. The fusion enzymes were successfully immobilized (>99% of bound protein) via covalent bonding onto epoxy-activated beads. To the best of our knowledge, this is the first example where fused enzymes are used to catalyze transesterification reactions for polymer synthesis purposes. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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