Muller_2005_Macromol.Rapid.Commun_26_1400

Reference

Title : Enzymatic degradation of poly(ethylene terephthalate):rapid hydrolyse using a hydrolase from T.fusca - Muller_2005_Macromol.Rapid.Commun_26_1400
Author(s) : R.J. Muller, H. Schrader, J. Profe, K. Dresler, W.D. Deckwer , Muller RJ , Schrader H , Profe J , Dresler K , Deckwer WD
Ref : Macromol Rapid Commun , 26 :1400 , 2005
Abstract :

It is demonstrated that PET, which is usually regarded as non-biodegradable, can effectively be depolymerized by a hydrolase from the actinomycete Thermobifida fusca. Erosion rates of 8 to 17 m per week were obtained upon incubation at 55 C. Lipases from Pseudomonas sp. and Candida antarctica did not degrade PET under comparable conditions. The influences of crystallinity, melting point, and glass transition temperature on the enzymatic attack on PET, PBT, and PHB are discussed.

PubMedSearch : Muller_2005_Macromol.Rapid.Commun_26_1400
PubMedID:
Gene_locus related to this paper: thefu-1831 , thefu-q6a0i3

Related information

Substrate BETEB    Polyethylene-terephthalate
Gene_locus thefu-1831    thefu-q6a0i3

Citations formats

R.J. Muller, H. Schrader, J. Profe, K. Dresler, W.D. Deckwer, Muller RJ, Schrader H, Profe J, Dresler K, Deckwer WD (2005)
Enzymatic degradation of poly(ethylene terephthalate):rapid hydrolyse using a hydrolase from T.fusca
Macromol Rapid Commun 26 :1400

R.J. Muller, H. Schrader, J. Profe, K. Dresler, W.D. Deckwer, Muller RJ, Schrader H, Profe J, Dresler K, Deckwer WD (2005)
Macromol Rapid Commun 26 :1400