dc.contributor.author | Littlechild, JA | |
dc.date.accessioned | 2016-06-16T06:48:05Z | |
dc.date.issued | 2015-10-13 | |
dc.description.abstract | This article will discuss the importance of specific extremophilic enzymes for applications in industrial biotechnology. It will specifically address those enzymes that have applications in the area of biocatalysis. Such enzymes now play an important role in catalyzing a variety of chemical conversions that were previously carried out by traditional chemistry. The biocatalytic process is carried out under mild conditions and with greater specificity. The enzyme process does not result in the toxic waste that is usually produced in a chemical process that would require careful disposal. In this sense, the biocatalytic process is referred to as carrying out "green chemistry" which is considered to be environmentally friendly. Some of the extremophilic enzymes to be discussed have already been developed for industrial processes such as an l-aminoacylase and a γ-lactamase. The industrial applications of other extremophilic enzymes, including transaminases, carbonic anhydrases, dehalogenases, specific esterases, and epoxide hydrolases, are currently being assessed. Specific examples of these industrially important enzymes that have been studied in the authors group will be presented in this review. | en_GB |
dc.description.sponsorship | The author would like to thank the University of Exeter, the Wellcome Trust, the BBSRC, the EPSRC, and the Technology Strategy Board, UK, for sponsoring research in the JL Laboratories at the Exeter Biocatalysis Centre. The EU Framework 7 grant “HotZyme” entitled Systematic Screening of Organisms from Hot Environments, Grant Number 265933, is thanked for supporting studies on the isolation of the metagenomes from Russia and China where the novel thermophilic limonene epoxide hydrolases were isolated and for the identification of the first thermophilic Planctomycetes species where the novel thermophilic esterase was identified. This EU project sponsored the research to clone, overexpress, and biochemically and structurally characterize these three new enzymes to allow their potential commercial exploitation. JL would like to thank all of the collaborators, postdoctoral fellows, and students who have contributed to the research work covered in this paper. | en_GB |
dc.identifier.citation | Vol. 3, pp. 161 - | en_GB |
dc.identifier.doi | 10.3389/fbioe.2015.00161 | |
dc.identifier.uri | http://hdl.handle.net/10871/22125 | |
dc.language.iso | en | en_GB |
dc.publisher | Frontiers Media | en_GB |
dc.relation.url | http://www.ncbi.nlm.nih.gov/pubmed/26528475 | en_GB |
dc.relation.url | http://journal.frontiersin.org/article/10.3389/fbioe.2015.00161/full | en_GB |
dc.rights | This is the final version of the article. Available from Frontiers Media via the DOI in this record. | en_GB |
dc.subject | carbonic anhydrase | en_GB |
dc.subject | dehalogenase | en_GB |
dc.subject | epoxide hydrolase | en_GB |
dc.subject | esterase | en_GB |
dc.subject | l-aminoacylase | en_GB |
dc.subject | transaminase | en_GB |
dc.subject | γ-lactamase | en_GB |
dc.title | Enzymes from Extreme Environments and Their Industrial Applications. | en_GB |
dc.type | Article | en_GB |
dc.date.available | 2016-06-16T06:48:05Z | |
exeter.place-of-publication | Switzerland | |
dc.description | Published online | en_GB |
dc.description | Journal Article | en_GB |
dc.description | Review | en_GB |
dc.identifier.eissn | 2296-4185 | |
dc.identifier.journal | Frontiers in Bioengineering and Biotechnology | en_GB |