Thermobifida fusca, cutinase

Cutinase Thermobifida fusca Release of oligomers, hydrophilicity, XPS, Maldi-Tof, K/S values after dying [24, 37, 54, 55, 57]... 

Abstract The functionalization of synthetic polymers such as poly(ethylene terephthalate) to improve their hydrophilicity can be achieved biocatalytically using hydrolytic enzymes. A number of cutinases, lipases, and esterases active on polyethylene terephthalate have been identified and characterized. Enzymes from Fusarium solani, Thermomyces insolens, T. lanuginosus, Aspergillus oryzae, Pseudomonas mendocina, and Thermobifida fusca have been studied in detail. Thermostable biocatalysts hydrolyzing poly(ethylene terephthalate) are promising candidates for the further optimization of suitable biofunctionalization processes for textile finishing, technical, and biomedical applications. 

Chen S, Su L, Billig S, Zimmermann W, Chen J, Wu J (2010) Biochemical characterization of the cutinases from Thermobifida fusca. J Mol Catal B Enzym 63 121-127... 

PPT) were treated with polyesterases from Thermomyces lanuginosus, Penicillium citrinum, Thermobifida fusca and Fusarium solani pisi, and the cutinase from Thermobifida fusca was found to release the highest amounts of hydrolysis prodncts from PPT materials [37]. The Thermobifida fusca enzyme hydrolysed both PPT fibres and films, whereas the lipase from Thermomyces lanuginosus was only able to hydrolyse the fibres. Due to the higher surface area, fibres are more easily attacked by enzymes than films. 

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