dc.contributor.author | Littlechild, JA | |
dc.date.accessioned | 2017-06-09T14:34:06Z | |
dc.date.issued | 2017-04-11 | |
dc.description.abstract | 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. | en_GB |
dc.description.sponsorship | The author would like to thank the University of Exeter, the Wellcome Trust, the BBSRC, EPSRC and Technology Strategy Board, UK, for sponsoring research in the JAL group at the Exeter Biocatalysis Centre. The BBSRC funded ERA-IB grant BB/L002035/1 and the University of Exeter are thanked for support. Thanks are also given to the EU Framework 7 grant ‘HOTZYME’ entitled Systematic Screening of Organisms from Hot Environments, Grant Number 265933. | en_GB |
dc.identifier.citation | Vol. 44 (4), pp. 711 - 720 | en_GB |
dc.identifier.doi | 10.1007/s10295-017-1920-5 | |
dc.identifier.uri | http://hdl.handle.net/10871/27922 | |
dc.language.iso | en | en_GB |
dc.publisher | Springer Verlag for Society for Industrial Microbiology | en_GB |
dc.relation.url | https://www.ncbi.nlm.nih.gov/pubmed/28401315 | en_GB |
dc.rights | © The Author(s) 2017. Open Access. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. | en_GB |
dc.subject | Carbonic anhydrases | en_GB |
dc.subject | Epoxide hydrolases | en_GB |
dc.subject | Esterases | en_GB |
dc.subject | Lactonases | en_GB |
dc.subject | Thermophilic enzymes | en_GB |
dc.title | Improving the 'tool box' for robust industrial enzymes. | en_GB |
dc.type | Article | en_GB |
dc.date.available | 2017-06-09T14:34:06Z | |
exeter.place-of-publication | Germany | en_GB |
dc.description | This is the final version of the article. Available from Springer Verlag via the DOI in this record. | en_GB |
dc.identifier.journal | Journal of Industrial Microbiology and Biotechnology | en_GB |