Improving the 'tool box' for robust industrial enzymes

被引:27
作者
Littlechild, J. A. [1 ]
机构
[1] Univ Exeter, Coll Life & Environm Sci, Biosci, Henry Wellcome Bldg Biocatalysis,Stocker Rd, Exeter EX4 4QD, Devon, England
基金
英国工程与自然科学研究理事会; 英国生物技术与生命科学研究理事会; 英国惠康基金;
关键词
Thermophilic enzymes; Esterases; Lactonases; Epoxide hydrolases; Carbonic anhydrases; ARCHAEON SULFOLOBUS-SOLFATARICUS; ENTNER-DOUDOROFF PATHWAY; ALPHA-CARBONIC ANHYDRASE; COMPLETE GENOME SEQUENCE; X-RAY-STRUCTURE; CRYSTAL-STRUCTURE; THERMOSTABLE ESTERASE; EPOXIDE HYDROLASE; CATALYTIC MECHANISM; PROMISCUITY;
D O I
10.1007/s10295-017-1920-5
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
The speed of sequencing of microbial genomes and metagenomes is providing an ever increasing resource for the identification of new robust biocatalysts with industrial applications for many different aspects of industrial biotechnology. Using 'natures catalysts' provides a sustainable approach to chemical synthesis of fine chemicals, general chemicals such as surfactants and new consumer-based materials such as biodegradable plastics. This provides a sustainable and 'green chemistry' route to chemical synthesis which generates no toxic waste and is environmentally friendly. In addition, enzymes can play important roles in other applications such as carbon dioxide capture, breakdown of food and other waste streams to provide a route to the concept of a 'circular economy' where nothing is wasted. The use of improved bioinformatic approaches and the development of new rapid enzyme activity screening methodology can provide an endless resource for new robust industrial biocatalysts.This mini-review will discuss several recent case studies where industrial enzymes of 'high priority' have been identified and characterised. It will highlight specific hydrolase enzymes and recent case studies which have been carried out within our group in Exeter.
引用
收藏
页码:711 / 720
页数:10
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