解聚
聚酯纤维
聚对苯二甲酸乙二醇酯
聚对苯二甲酸丁二醇酯
对苯二甲酸
生物降解
材料科学
角质酶
有机化学
基质(水族馆)
吸附
高分子化学
化学
化学工程
水解
复合材料
工程类
地质学
海洋学
作者
Umer Abid,Gordon Sun,Ya‐Hue Valerie Soong,Alexandria Williams,Allen C. Chang,Christian Ayafor,Akanksha Patel,Hsi‐Wu Wong,Margaret J. Sobkowicz,Dongming Xie
标识
DOI:10.1016/j.bej.2023.109074
摘要
Millions of tons of waste polyester plastics, including polyethylene terephthalate (PET), polytrimethylene terephthalate (PTT), and polybutylene terephthalate (PBT), end up in the environment as soil and water contaminants. Recent advances in enzymatic polyester degradation have motivated researchers toward the biorecycling of plastic wastes. Leaf-branch compost cutinase (LCC) enzymes have been proven to be effective in the biodegradation of PET. This study focuses on enzymatic depolymerization of waste PET, PTT, and PBT materials by using an ICCG variant of LCC (LCCICCG) produced from Escherichia coli BL21(DE3). The degradation efficiency of the polyesters was determined by the monomer terephthalic acid (TPA) released from the depolymerization reaction. It was found that the most efficient depolymerization was achieved for PET, followed by PTT and PBT. A kinetic model based on Langmuir adsorption and the Michaelis-Menten equation was developed to describe the enzymatic depolymerization of PET, PTT, and PBT with various enzyme and substrate loadings. The model simulation results revealed that the LCCICCG enzyme loading should be linearly increased as the work capacity of the polyester substrate increases. A specific enzyme loading of 0.91 mg/g PET is suggested to achieve 90% depolymerization of PET within three days. The experimental data and model simulation results can be used to help further engineer the enzyme and process to achieve a complete biodegradation of polyester wastes at a large scale.
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