Microbial degradation of polyurethane, polyester polyurethanes and polyether polyurethanes

被引:189
作者
Nakajima-Kambe, T [1 ]
Shigeno-Akutsu, Y [1 ]
Nomura, N [1 ]
Onuma, F [1 ]
Nakahara, T [1 ]
机构
[1] Univ Tsukuba, Inst Appl Biochem, Ibaraki, Osaka 3058572, Japan
关键词
D O I
10.1007/s002530051373
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
Polyurethane (PUR) is a polymer derived from the condensation of polyisocyanate and polyol and it is widely used as a base material in various industries. PUR, in particular, polyester PUR, is known to be vulnerable to microbial attack. Recently, environmental pollution by plastic wastes has become a serious issue and polyester PUR had attracted attention because of its biodegradability. There are many reports on the degradation of polyester PUR by microorganisms, especially by fungi. Microbial degradation of polyester PUR is thought to be mainly due to the hydrolysis of ester bonds by esterases. Recently, polyester-PUR-degrading enzymes have been purified and their characteristics reported. Among them, a solid-polyester-PUR-degrading enzyme (PUR esterase) derived from Comamonas acid-ovorans ans TB-35 had unique characteristics. This enzyme has a hydrophobic PUR-surface-binding domain and a catalytic domain, and the surface-binding domain was considered as being essential for PUR degradation. This hydrophobic surface-binding domain is also observed in other solid-polyester-degrading enzymes such as poly(hydroxyalkanoate) (PHA) depolymerases. There was no significant homology between the amino acid sequence of PUR esterase and that of PHA depolymerases, except in the hydrophobic surface-binding region. Thus, PUR esterase and PHA depolymerase are probably different in terms of their evolutionary origin and it is possible that PUR esterases come to be classified as a new solid-polyester-degrading enzyme family.
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页码:134 / 140
页数:7
相关论文
共 41 条
[1]  
Akutsu Y, 1998, APPL ENVIRON MICROB, V64, P62
[2]   Poly(3-hydroxybutyrate) depolymerases bind to their substrate by a C-terminal located substrate binding site [J].
Behrends, A ;
Klingbeil, B ;
Jendrossek, D .
FEMS MICROBIOLOGY LETTERS, 1996, 143 (2-3) :191-194
[3]   THE MOLECULAR EVOLUTION OF GENES AND PROTEINS - A TALE OF 2 SERINES [J].
BRENNER, S .
NATURE, 1988, 334 (6182) :528-530
[4]   BIODEGRADATION OF A COLLOIDAL ESTER-BASED POLYURETHANE BY SOIL FUNGI [J].
CRABBE, JR ;
CAMPBELL, JR ;
THOMPSON, L ;
WALZ, SL ;
SCHULTZ, WW .
INTERNATIONAL BIODETERIORATION & BIODEGRADATION, 1994, 33 (02) :103-113
[5]  
CYGLER M, 1993, PROTEIN SCI, V2, P366
[6]   FUNGAL SUSCEPTIBILITY OF POLYURETHANES [J].
DARBY, RT ;
KAPLAN, AM .
APPLIED MICROBIOLOGY, 1968, 16 (06) :900-&
[7]   DECOMPOSTION OF POLYURETHANE IN A GARBAGE LANDFILL LEAKAGE WATER AND BY SOIL-MICROORGANISMS [J].
FILIP, Z .
EUROPEAN JOURNAL OF APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 1978, 5 (03) :225-231
[8]   EFFECT OF LIMITED TRYPTIC MODIFICATION OF A BACTERIAL POLY(3-HYDROXYBUTYRATE) DEPOLYMERASE ON ITS CATALYTIC ACTIVITY [J].
FUKUI, T ;
NARIKAWA, T ;
MIWA, K ;
SHIRAKURA, Y ;
SAITO, T ;
TOMITA, K .
BIOCHIMICA ET BIOPHYSICA ACTA, 1988, 952 (02) :164-171
[9]   FIBRONECTIN TYPE III-LIKE SEQUENCES AND A NEW DOMAIN TYPE IN PROKARYOTIC DEPOLYMERASES WITH INSOLUBLE SUBSTRATES [J].
HANSEN, CK .
FEBS LETTERS, 1992, 305 (02) :91-96
[10]  
JANSEN B, 1991, ZBL BAKT-INT J MED M, V276, P36