Fully renewable polyesters via polycondensation catalyzed by Thermobifida cellulosilytica cutinase 1: an integrated approach
Fully renewable polyesters via polycondensation catalyzed by Thermobifida cellulosilytica cutinase 1: an integrated approach
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DOI：
10.1039/c6gc02142e
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发表时间：
2017-01-21
期刊：
影响因子：
9.8
通讯作者：
Gardossi, Lucia
中科院分区：
文献类型：
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作者：
Pellis, Alessandro;Ferrario, Valerio;Gardossi, Lucia
本研究全面解决了通过可持续工艺生产聚酯的问题，同时使用完全可再生的原料和生物催化剂。利用Thermobifida cellulosilytica的角质酶1 （Thc_cut1）在无溶剂和薄膜条件下催化生物基己二酸二甲酯与不同二醇的缩聚反应。将该生物催化剂高效地固定在以碾碎稻壳为载体的完全可再生廉价载体上。多因素因子设计表明，Thc_cut1对系统中存在的水不太敏感，与来自南极念珠菌（CaLB）的脂肪酶B相比，它在较温和的条件下（50摄氏度；535毫巴）有效工作，从而实现了节能。Thermobifida cellulosilytica的角质酶1 （Thc_cut1）的实验和计算研究揭示了使该丝氨酸水解酶在缩聚反应中高效的结构和功能特征。使用BioGPS工具进行的生物信息学分析指出了与CaLB的功能相似性，并为未来的工程研究提供了指导，例如，在Thc_cut1支架中引入不同的混杂活性。结果为充分利用酶在环境和经济上可持续的酶缩聚反应设定了坚实的前提。
The present study addresses comprehensively the problem of producing polyesters through sustainable processes while using fully renewable raw materials and biocatalysts. Polycondensation of bio-based dimethyl adipate with different diols was catalyzed by cutinase 1 from Thermobifida cellulosilytica (Thc_cut1) under solvent free and thin-film conditions. The biocatalyst was immobilized efficiently on a fully renewable cheap carrier based on milled rice husk. A multivariate factorial design demonstrated that Thc_cut1 is less sensitive to the presence of water in the system and it works efficiently under milder conditions (50 degrees C; 535 mbar) when compared to lipase B from Candida antarctica (CaLB), thus enabling energy savings. Experimental and computational investigations of cutinase 1 from Thermobifida cellulosilytica (Thc_cut1) disclosed structural and functional features that make this serine-hydrolase efficient in polycondensation reactions. Bioinformatic analysis performed with the BioGPS tool pointed out functional similarities with CaLB and provided guidelines for future engineering studies aiming, for instance, at introducing different promiscuous activities in the Thc_cut1 scaffold. The results set robust premises for a full exploitation of enzymes in environmentally and economically sustainable enzymatic polycondensation reactions.