聚对苯二甲酸乙二醇酯
吸附
单层
聚合物
酶
基质(水族馆)
水解
化学
离解常数
配体(生物化学)
聚乙烯
朗缪尔
合理设计
化学工程
有机化学
材料科学
生物化学
纳米技术
受体
生物
生态学
复合材料
工程类
作者
Silke Flindt Badino,Jenny Arnling Bååth,Kim Borch,Kenneth Jensen,Peter Westh
标识
DOI:10.1016/j.enzmictec.2021.109937
摘要
Polyethylene terephthalate (PET) degrading enzymes have recently obtained an increasing interest as a means to decompose plastic waste. Here, we have studied the binding of three PET hydrolases on a suspended PET powder under conditions of both enzyme- and substrate excess. A Langmuir isotherm described the binding process reasonably and revealed a prominent affinity for the PET substrate, with dissociation constants consistently below 150 nM. The saturated substrate coverage approximately corresponded to a monolayer on the PET surface for all three enzymes. No distinct contributions from specific ligand binding in the active site could be identified, which points towards adsorption predominantly driven by non-specific interactions in contrast to enzymes naturally evolved for the breakdown of insoluble polymers. However, we observed a correlation between the progression of enzymatic hydrolysis and increased binding capacity, probably due to surface modifications of the PET polymer over time. Our results provide functional insight, suggesting that rational design should target the specific ligand interaction in the active site rather than the already high, general adsorption capacity of these enzymes.
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