Enzymatic hydrolysis of PTT polymers and oligomers
| Autor: | Franz Kaufmann, Georg Gübitz, Richard Kotek, Artur Cavaco-Paulo, Stefan Mitsche, Anita Eberl, Sonja Heumann |
|---|---|
| Přispěvatelé: | Universidade do Minho |
| Rok vydání: | 2007 |
| Předmět: |
0106 biological sciences
Cutinase Polymers Dimer Polyester Bioengineering 02 engineering and technology 01 natural sciences Applied Microbiology and Biotechnology Oligomer Fungal Proteins chemistry.chemical_compound Hydrolysis Crystallinity 010608 biotechnology Enzymatic hydrolysis Polymer chemistry Polyesterase Lipase Science & Technology biology Chemistry Polyethylene Terephthalates Esterases General Medicine 021001 nanoscience & nanotechnology Poly(trimethylene terephthalate) biology.protein 0210 nano-technology Biotechnology |
| Zdroj: | Repositório Científico de Acesso Aberto de Portugal Repositório Científico de Acesso Aberto de Portugal (RCAAP) instacron:RCAAP |
| ISSN: | 0168-1656 |
| Popis: | Article in Press Oligomers and polymers (film, fabrics) of the linear aromatic polyester poly(trimethylene terephthalate) (PTT) were treated with polyesterases from Thermomyces lanuginosus, Penicillium citrinum, Thermobifida fusca and Fusarium solani pisi. The cutinase from T. fusca was found to release the highest amounts of hydrolysis products from PTT materials and was able to open and hydrolyse a cyclic PTT dimer according to RP-HPLC–UV detection. In contrast, the lipase from T. lanuginosus also showed activity on the PTT fibres and on bis(3-hydroxypropyl) terephthalate (BHPT) but was not able to hydrolyse the polymer film, mono(3-hydroxypropyl) terephthalate (MHPT) nor the cyclic dimer of PTT. As control enzymes inhibited with mercury chloride were used. Surface hydrophilicity changes were investigated with contact angle measurements and the degree of crystallinity changes were determined with DSC. |
| Databáze: | OpenAIRE |
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