Enzymatic hydrolysis of PTT polymers and oligomers

被引：66
作者：
Eberl, A. [1 ,2 ]
Heumann, S. [1 ,2 ]
Kotek, R. [4 ]
Kaufmann, F. [5 ]
Mitsche, S. [3 ]
Cavaco-Paulo, A. [6 ]
Guebitz, G. M. [1 ]
机构：
[1] Graz Univ Technol, Dept Environm Biotechnol, A-8010 Graz, Austria
[2] Res Ctr Appl Biocatalysis, A-8010 Graz, Austria
[3] Graz Univ Technol, Res Inst Electron Microscopy, A-8010 Graz, Austria
[4] N Carolina State Univ, Dept Text Engn Chem & Sci, Coll Text, Raleigh, NC 27695 USA
[5] CIBA Inc, Basel, Switzerland
[6] Univ Minho, Dept Text Engn, P-4800 Guimaraes, Portugal
来源：
JOURNAL OF BIOTECHNOLOGY | 2008年 / 135卷 / 01期
关键词：
poly(trimethylene terephthalate); polyester; polyesterase; cutinase;
D O I：
10.1016/j.jbiotec.2008.02.015
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
Oligomers and polymers (film, fabrics) of the linear aromatic polyester poly(trimethylene terephthalate) (PTT) were treated with polyesterases from Thermomyces lanuginosus, Penicillium citrinum, Thermobifida fusca and Fusarium solani pisi. The cutinase from T fusca was found to release the highest amounts of hydrolysis products from PTT materials and was able to open and hydrolyse a cyclic PTT dimer according to RP-HPLC-UV detection. In contrast, the lipase from T lanuginosus also showed activity on the PTT fibres and on bis(3-hydroxypropyl) terephthalate (BHPT) but was not able to hydrolyse the polymer film, mono(3-hydroxypropyl) terephthalate (MHPT) nor the cyclic dimer of PTT. As control enzymes inhibited with mercury chloride were used. Surface hydrophilicity changes were investigated with contact angle measurements and the degree of crystallinity changes were determined with DSC. (C) 2008 Elsevier B.V. All rights reserved.
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收藏
页码：45 / 51
页数：7
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