Towards a biocatalytic solution for the recycling of carbon fibre composites

利用酶作为生物催化剂降解和回收（多）晶体和固体材料（如纤维素和木质素、塑料和碳纤维复合材料）的兴趣日益浓厚。酶可以被认为是传统化学催化剂的相对环保、具有成本效益和可持续的替代品，因为它们可以在温和的条件下（环境温度、压力、pH等）和水等良性溶剂下发挥作用。然而，酶在非天然底物上的鉴定、工程和实验室进化仍然存在挑战，特别是当底物不可溶时。该博士项目旨在：(i)研究结合和降解（多）晶体和固体材料的酶的结构/功能关系和机制特征；制定可用于更可靠地设计这些酶以改善活性和（或）扩大其底物范围的设计规则；（iii）利用这种数据驱动方法来设计酶，以更好地降解聚合物和复合材料，特别关注水解酶和双马来酰亚胺（BMI）纤维复合材料。这个博士项目将采用跨学科的方法，结合计算化学、酶工程和材料科学，是曼彻斯特大学和BAE系统公司的合作项目。该项目将以曼彻斯特生物技术研究所（MIB）和曼彻斯特大学亨利·罗伊斯研究所为基础，将以我们研究蛋白质-固体相互作用的经验为基础，为PETase和其他酶开发酶工程平台，并利用计算化学研究酶的机制。

There is substantial and growing interest in the use of enzymes as biocatalysts for the degradation and recycling of (poly)crystalline and solid materials such as cellulose and lignin, plastics, and carbon fibre composites. Enzymes can be considered relatively environmentally friendly, cost-effective and sustainable alternatives to conventional chemical catalysts, since they can function under mild conditions (ambient temperature, pressure, pH etc.) and benign solvents such as water. However, challenges remain in the identification, engineering and laboratory evolution of enzymes to work on non-natural substrates, particularly when the substrates are not soluble. This PhD project aims to: (i) Investigate the structure/function relationships and mechanistic features of enzymes that bind to and degrade (poly)crystalline and solid materials; (ii) Develop design rules that can be used to more reliably engineer these enzymes to improve activity and/or expand their substrate scope; (iii) Use this data-drive approach to engineer enzymes to better degrade polymers and composite materials, with a specific focus on hydrolytic enzymes and bismaleimide (BMI)-fibre composites. This PhD project will use an interdisciplinary approach combining computational chemistry, enzyme engineering and materials science and is a collaboration between the University of Manchester and BAE Systems. The project will be based in the Manchester Institute of Biotechnology (MIB) and Henry Royce Institute at the University of Manchester and will build on our experience of studying protein-solid interactions, developing an enzyme engineering platform for PETase and other enzymes, and studying enzyme mechanism using computational chemistry.