Document Detail


Postgenomic approaches to using corynebacteria as biocatalysts.
MedLine Citation:
PMID:  22803796     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Corynebacterium glutamicum exhibits numerous ideal intrinsic attributes as a factory of primary and secondary metabolites. The versatile capabilities of this organism have long been implemented at the industrial scale to produce an array of amino acids at high yields and conversion rates, thereby enabling the development of an entire industry. The postgenomic era provides a new technological platform not only to further optimize the intrinsic attributes of C. glutamicum whole cells as biocatalysts, but also to dramatically expand the product portfolio that can be manufactured by this organism, from amino acids to commodity chemicals. This review addresses the methods and strain optimization strategies enabled by genomic information and associated techniques. Their implementation has provided important additional incremental improvements to the economics of industry-scale manufacturing in which C. glutamicum and its episomal elements are used as a performing host-vector system.
Authors:
Alain A Vertès; Masayuki Inui; Hideaki Yukawa
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Publication Detail:
Type:  Journal Article; Review     Date:  2012-07-09
Journal Detail:
Title:  Annual review of microbiology     Volume:  66     ISSN:  1545-3251     ISO Abbreviation:  Annu. Rev. Microbiol.     Publication Date:  2012  
Date Detail:
Created Date:  2012-09-21     Completed Date:  2013-01-30     Revised Date:  2014-04-11    
Medline Journal Info:
Nlm Unique ID:  0372370     Medline TA:  Annu Rev Microbiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  521-50     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Biotechnology / methods
Corynebacterium glutamicum / enzymology*,  genetics*,  metabolism
Enzymes / genetics*,  metabolism*
Industrial Microbiology / methods
Metabolic Engineering / methods
Metabolic Networks and Pathways / genetics
Chemical
Reg. No./Substance:
0/Enzymes

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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