Abstract:
OBJECTIVES:To improve the production of α-ketoglutaric acid (α-KG) from L-glutamate by whole-cell biocatalysis. RESULTS:A novel and highly active L-glutamate oxidase, SmlGOX, from Streptomyces mobaraensis was overexpressed and purified. The recombinant SmlGOX was approx. 64 kDa by SDS-PAGE. SmlGOX had a maximal activity of 125 ± 2.7 U mg-1 at pH 6.0, 35 oC. The apparent Km and Vmax values of SmlGOX were 9.3 ± 0.5 mM and 159 ± 3 U mg-1, respectively. Subsequently, a co-expression plasmid containing the SmlGOX and KatE genes was constructed to remove H2O2, and the protein levels of SmlGOX were improved by codon optimization. Finally, by optimizing the whole-cell transformation conditions, the production of α-KG reached 77.4 g l-1 with a conversion rate from L-glutamate of 98.5% after 12 h. CONCLUSIONS:An efficient method for the production of α-KG was established in the recombinant Escherichia coli, and it has a potential prospect in industrial application.
journal_name
Biotechnol Lettjournal_title
Biotechnology lettersauthors
Liu Q,Ma X,Cheng H,Xu N,Liu J,Ma Ydoi
10.1007/s10529-017-2314-5subject
Has Abstractpub_date
2017-06-01 00:00:00pages
913-919issue
6eissn
0141-5492issn
1573-6776pii
10.1007/s10529-017-2314-5journal_volume
39pub_type
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