New model substrates for enzymes hydrolysing polyethyleneterephthalate and polyamide fibres.
Recently the potential of enzymes for surface hydrophilisation and/or functionalisation of polyethyleneterephthalate (PET) and polyamide (PA) has been discovered. However, there was no correlation between enzyme class/activity (e.g. esterase, lipase, cutinase) and surface hydrolysis of these polymers and consequently no simple assay to estimate this capability. Enzymes active on the model substrates bis (benzoyloxyethyl) terephthalate and adipic acid bishexyl-amide, were also capable of increasing the hydrophilicity of PET and PA. When dosed at the identical activity on 4-nitrophenyl butyrate, only enzymes from Thermobifida fusca, Aspergillus sp., Beauveria sp. and commercial enzymes (TEXAZYME PES sp5 and Lipase PS) increased the hydrophilicity of PET fibres while other esterases and lipases did not show any effect. Activity on PET correlated with the activity on the model substrate. Hydrophilicity of fibres was greatly improved based on increases in rising height of up to 4.3 cm and the relative decrease of water absorption time between control and sample of the water was up to 76%. Similarly, enzymes increasing the hydrophilicity of PA fibres such as from Nocardia sp., Beauveria sp. and F. solani hydrolysed the model substrate; however, there was no common enzyme activity (e.g. protease, esterase, amidase) which could be attributed to all these enzymes.
Heumann
Sonja
S
Research Centre Applied Biocatalysis, Petersgasse 14, A-8010 Graz, Austria.
Eberl
Anita
A
Pobeheim
Herbert
H
Liebminger
Stefan
S
Fischer-Colbrie
Gudrun
G
Almansa
Eva
E
Cavaco-Paulo
Artur
A
Gübitz
Georg M
GM
D000192:Actinomycetales / Q000201:enzymology; D000581:Amidohydrolases / Q000378:metabolism; D001230:Aspergillus / Q000201:enzymology; D052982:Beauveria / Q000201:enzymology; D001709:Biotechnology; D004798:Enzymes / Q000378:metabolism*; D004950:Esterases / Q000378:metabolism; D005670:Fusarium / Q000201:enzymology; D006868:Hydrolysis; D008956:Models, Chemical; D009615:Nocardia / Q000201:enzymology; D009757:Nylons / Q000737:chemistry / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism; D011093:Polyethylene Terephthalates / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity
D004798:Enzymes; D009757:Nylons; D011093:Polyethylene Terephthalates; D004950:Esterases; D010447:Peptide Hydrolases; D000581:Amidohydrolases