A novel aryl acylamidase from Nocardia farcinica hydrolyses polyamide
| Autor: | Anita Eberl, Sonja Heumann, Franz Kaufmann, Georg M. Guebitz, Gudrun Fischer-Colbrie, Artur Cavaco-Paulo, Herbert Pobeheim, Doris Ribitsch |
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| Přispěvatelé: | Universidade do Minho |
| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
Stereochemistry
Polymers Molecular Sequence Data Bioengineering 02 engineering and technology Applied Microbiology and Biotechnology Nocardia Amidase Amidohydrolases 03 medical and health sciences Hydrolysis Hydrolase Amidase activity Organic chemistry Caprolactam Amino Acid Sequence Phylogeny 030304 developmental biology Nocardia farcinica 0303 health sciences Science & Technology biology Sequence Homology Amino Acid Chemistry 021001 nanoscience & nanotechnology biology.organism_classification Molecular Weight Butyrates Kinetics Protein Subunits Polyamide Actinomycetales 0210 nano-technology Hydrophobic and Hydrophilic Interactions Sequence Alignment Biotechnology |
| Zdroj: | Repositório Científico de Acesso Aberto de Portugal Repositório Científico de Acesso Aberto de Portugal (RCAAP) instacron:RCAAP |
| Popis: | An alkali stable polyamidase was isolated from a new strain of Nocardia farcinica. The enzyme consists of four subunits with a total molecular weight of 190 kDa. The polyamidase cleaved amide and ester bonds of water insoluble model substrates like adipic acid bishexylamide and bis(benzoyloxyethyl)terephthalate and hydrolyzed different soluble amides to the corresponding acid. Treatment of polyamide 6 with this amidase led to an increased hydrophilicity based on rising height and tensiometry measurements and evidence of surface hydrolysis of polyamide 6 is shown. In addition to amidase activity, the enzyme showed activity on p-nitrophenylbutyrate. On hexanoamide the amidase exhibited a Km value of 5.5 mM compared to 0.07 mM for p-nitroacetanilide. The polyamidase belongs to the amidase signature family and is closely related to aryl acylamidases from different strains/species of Nocardia and to the 6-aminohexanoate-cyclic dimer hydrolase (EI) from Arthrobacter sp. KI72. We would like to thank Markus List for measuring of the hydrophilicity of PA fabrics. The research was financed by the Commission of the European Union (GRD2000-30110 BIOSNYTEX), the Austrian FFG, the SFG, the City of Graz, and the Province of Styria. |
| Databáze: | OpenAIRE |
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