Document Detail

Engineering of an N-acetylneuraminic acid synthetic pathway in Escherichia coli.
MedLine Citation:
PMID:  23018051     Owner:  NLM     Status:  Publisher    
N-acetylneuraminic acid (NeuAc) has recently drawn much attention owing to its wide applications in many aspects. Besides extraction from natural materials, production of NeuAc was recently focused on enzymatic synthesis and whole-cell biocatalysis. In this study, we designed an artificial NeuAc biosynthetic pathway through intermediate N-acetylglucosamine 6-phosphate in Escherichia coli. In this pathway, N-acetylglucosamine 2-epimerase (slr1975) and glucosamine-6-phosphate acetyltransferase (GNA1) were heterologously introduced into E. coli from Synechocystis sp. PCC6803 and Saccharomyces cerevisiae EBY100, respectively. By derepressing the feedback inhibition of glucosamine-6-phosphate synthase, increasing the accumulation of N-acetylglucosamine and pyruvate, and blocking the catabolism of NeuAc, we were able to produce 1.62gl(-1) NeuAc in recombinant E. coli directly from glucose. The NeuAc yield reached 7.85gl(-1) in fed-batch fermentation. This process offered an efficient fermentative method to produce NeuAc in microorganisms using glucose as carbon source and can be optimized for further improvement.
Junhua Kang; Pengfei Gu; Yang Wang; Yikui Li; Fan Yang; Qian Wang; Qingsheng Qi
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-9-24
Journal Detail:
Title:  Metabolic engineering     Volume:  -     ISSN:  1096-7184     ISO Abbreviation:  Metab. Eng.     Publication Date:  2012 Sep 
Date Detail:
Created Date:  2012-9-28     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9815657     Medline TA:  Metab Eng     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2012. Published by Elsevier Inc.
State Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, P. R. China.
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