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Pseudomonas mendocina, cutinase

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. [Pg.97]

Gray GL, Power SD, Poulouse AJ (1995) Lipase from Pseudomonas Mendocina having cutinase activity. US Patent 5,389,536 Griffiths AD, Tawfik DS (2003) Directed evolution of an extremely fast phosphotriesterase by in vitro compartmentalization. EMBO J 22 24-35 Gusakov AV, Sinitsyn AP, Berlin AG, Markov AV, Ankudimova NV (2000) Surface hydrophobic amino acid residues in cellulase molecules as a structural factor responsible for their high denim-washing performance. Enzyme Microb Technol 27 664-671... [Pg.208]

See other pages where Pseudomonas mendocina, cutinase is mentioned: [Pg.28]    [Pg.26]    [Pg.98]    [Pg.111]    [Pg.28]    [Pg.26]    [Pg.98]    [Pg.111]    [Pg.125]    [Pg.120]    [Pg.104]   
See also in sourсe #XX -- [ Pg.111 ]



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