Document Detail

High-level production of bacillus subtilis glycine oxidase by fed-batch cultivation of recombinant Escherichia coli Rosetta (DE3).
MedLine Citation:
PMID:  17474758     Owner:  NLM     Status:  MEDLINE    
A fed-batch process for the high cell density cultivation of Escherichia coli Rosetta (DE3) and the production of the recombinant protein glycine oxidase (GOX) from Bacillus subtilis was developed. GOX is a deaminating enzyme that shares substrate specificity with d-amino acid oxidase and sarcosine oxidase and has great biotechnological potential. The B. subtilis gene coding for GOX was expressed in E. coli Rosetta under the strong inducible T7 promotor of the pET28a vector. Exponential feeding based on the specific growth rate and a starvation period for acetate utilization was used to control cell growth, acetate production, and reconsumption and glucose consumption during fed-batch cultivation. Expression of GOX was induced at three different cell densities (20, 40, and 60 g . L(-1)). When cells were induced at intermediate cell density, the amount of GOX produced was 20 U . g(-1) cell dry weight and 1154 U . L(-1) with a final intracellular protein concentration corresponding to approximately 37% of the total cell protein concentration. These values were higher than those previously published for GOX expression and also represent a drastic decrease of 26-fold in the cost of the culture medium.
Irene Martínez-Martínez; Christian Kaiser; Alexander Rohde; Andree Ellert; Francisco García-Carmona; Alvaro Sanchez-Ferrer; Reiner Luttmann
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-05-03
Journal Detail:
Title:  Biotechnology progress     Volume:  23     ISSN:  8756-7938     ISO Abbreviation:  Biotechnol. Prog.     Publication Date:    2007 May-Jun
Date Detail:
Created Date:  2007-06-01     Completed Date:  2007-08-06     Revised Date:  2011-10-03    
Medline Journal Info:
Nlm Unique ID:  8506292     Medline TA:  Biotechnol Prog     Country:  United States    
Other Details:
Languages:  eng     Pagination:  645-51     Citation Subset:  IM    
Department of Biochemistry and Molecular Biology-A, Faculty of Biology, University of Murcia, Campus Espinardo, E-30071 Murcia, Spain.
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MeSH Terms
Amino Acid Oxidoreductases / genetics,  metabolism*
Bacillus subtilis / enzymology*,  genetics
Bioreactors / microbiology
Cell Division / drug effects
Culture Media / pharmacology
Escherichia coli / genetics,  growth & development*,  metabolism
Gene Expression Regulation, Enzymologic / drug effects
Recombinant Proteins / biosynthesis,  metabolism*
Substrate Specificity
Reg. No./Substance:
0/Culture Media; 0/Recombinant Proteins; EC 1.4.-/Amino Acid Oxidoreductases; EC oxidase

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

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