Thermoacidophilic Sulfolobus species as source for extremozymes and as novel archaeal platform organisms.


Journal

Current opinion in biotechnology
ISSN: 1879-0429
Titre abrégé: Curr Opin Biotechnol
Pays: England
ID NLM: 9100492

Informations de publication

Date de publication:
10 2019
Historique:
received: 28 09 2018
revised: 29 01 2019
accepted: 09 02 2019
pubmed: 16 3 2019
medline: 11 2 2020
entrez: 16 3 2019
Statut: ppublish

Résumé

Archaea dominate extreme habitats and possess unique cellular and metabolic properties with novel or modified metabolic pathways and unusual enzymes. Thermoacidophilic Sulfolobus species and their thermo(acido)philic enzymes gained special attention due to their adaptation toward two extremes, high temperature (75-80°C) and low pH (pH 2-5), that matches harsh process conditions in industrial applications. For different Sulfolobus species versatile genetic systems have been established and significant metabolic and physiological information from classical biochemistry and genetic as well as poly-omics and systems biology approaches is available. Their ease of growth under aerobic or microaerophilic conditions and established fermentation technologies gaining high cell yields promote Sulfolobus as source for extremozymes and as valuable novel platform organism for industrial biotechnology.

Identifiants

pubmed: 30875666
pii: S0958-1669(18)30195-2
doi: 10.1016/j.copbio.2019.02.012
pii:
doi:

Types de publication

Journal Article Research Support, Non-U.S. Gov't Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

71-77

Informations de copyright

Copyright © 2019 Elsevier Ltd. All rights reserved.

Auteurs

Larissa Schocke (L)

Molecular Enzyme Technology and Biochemistry (MEB), Biofilm Centre, Centre for Water and Environmental Research (CWE), University of Duisburg-Essen, Universitätsstraße 5, 45141 Essen, Germany.

Christopher Bräsen (C)

Molecular Enzyme Technology and Biochemistry (MEB), Biofilm Centre, Centre for Water and Environmental Research (CWE), University of Duisburg-Essen, Universitätsstraße 5, 45141 Essen, Germany.

Bettina Siebers (B)

Molecular Enzyme Technology and Biochemistry (MEB), Biofilm Centre, Centre for Water and Environmental Research (CWE), University of Duisburg-Essen, Universitätsstraße 5, 45141 Essen, Germany. Electronic address: bettina.siebers@uni-due.de.

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Classifications MeSH