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Hydrolysis of Cutin by PET‐Hydrolases
Author(s) -
Korpecka Justyna,
Heumann Sonja,
Billig Susan,
Zimmermann Wolfgang,
Zinn Manfred,
Ihssen Julian,
CavacoPaulo Artur,
Guebitz Georg M.
Publication year - 2010
Publication title -
macromolecular symposia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.257
H-Index - 76
eISSN - 1521-3900
pISSN - 1022-1360
DOI - 10.1002/masy.201051047
Subject(s) - cutin , cutinase , hydrolysis , enzyme , chemistry , acyltransferases , lipase , chemical structure , polyester , carboxylesterase , biochemistry , organic chemistry , biosynthesis
Functionalisation of synthetic polymers by using enzymes has been recently demonstrated. The major advantage of enzymes over chemical processes lies in their surface specific and endo‐wise mode of action. Surface hydrophilisation of PET with lipases and cutinases leads to a dramatic increase of the surfacial acid and hydroxyl group content while conventional chemical treatment does not cause any change. However, this PET‐hydrolysing activity by enzymes from distinct classes has not yet been correlated to activity on natural polyesters. Here, we show that lipases, cutinases and a PHA‐depolymerase are all capable of hydrolysing PET, while only lipases and cutinases also hydrolysed cutin to various degrees. Lipases showed a higher specificity for terminal fatty acids while the cutinases preferred hydroxy fatty acids during cutin hydrolysis.