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Biological degradation of synthetic polyesters—Enzymes as potential catalysts for polyester recycling

机译:合成聚酯的生物降解—作为聚酯回收潜在催化剂的酶

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摘要

The depolymerization of polymers by enzymes is of great interest for biodegradable plastics, a group of materials which has been developed as an answer to increasing problems in plastics waste management. Polyesters play the dominant role in biodegradable polymers and recently a model of polyester degradation by hydrolyses (lipases) has been published. The chain mobility of the polymer chains proved to be the most relevant factor controlling polyester biodegradability, usually excluding many aromatic polyesters such as PET from biodegradation. Recently a new thermophilic hydrolase (activity optimum at 65℃) from Thermobifida fusca (TfH) was isolated, characterized and expressed in recombinant Escherichia coli. This enzyme is especially active in degrading polyesters containing aromatic constituents, and exhibits a 65% sequence similarity to a lipase from Streptomyces albus and combines characteristics of lipases and esterases. TfH is even capable to degrade commercial PET from beverage bottles. Specific modification of the active site of enzymes like TfH may open the door for enzymatic PET recycling in the future.
机译:对于生物可降解塑料而言,酶对聚合物进行解聚的兴趣很大,可降解塑料是为解决塑料废物管理中日益严重的问题而开发的一组材料。聚酯在可生物降解的聚合物中起主要作用,最近已公开了通过水解(脂肪酶)降解聚酯的模型。事实证明,聚合物链的链迁移率是控制聚酯生物降解能力的最重要因素,通常将许多芳族聚酯(例如PET)排除在生物降解范围之外。最近,从重组嗜热热菌(TfH)中分离出了一种新型嗜热水解酶(活性最适温度为65℃),并在重组大肠杆菌中进行了表征和表达。该酶在降解包含芳族成分的聚酯中特别有活性,并且与来自白色链霉菌的脂肪酶表现出65%的序列相似性,并且结合了脂肪酶和酯酶的特性。 TfH甚至能够降解饮料瓶中的商用PET。诸如TfH之类的酶的活性位点的特定修饰可能会在将来为酶促PET回收打开大门。

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