Abstract:
OBJECTIVE:To examine the role of a gene encoding flavin-containing monooxygenase (cFMO) from Corynebacterium glutamicum ATCC13032 when cloned and expressed in Escherichia coli for the production of indigo pigments. RESULTS:The blue pigments produced by recombinant E. coli were identified as indigo and indirubin. The cFMO was purified as a fused form with maltose-binding protein (MBP). The enzyme was optimal at 25 °C and pH 8. From absorption spectrum analysis, the cFMO was classified as a flavoprotein. FMO activity was strongly inhibited by 1 mM Cu(2+) and recovered by adding 1-10 mM EDTA. The enzyme catalyzed the oxidation of TMA, thiourea, and cysteamine, but not glutathione or cysteine. MBP-cFMO had an indole oxygenase activity through oxygenation of indole to indoxyl. The recombinant E. coli produced 685 mg indigo l(-1) and 103 mg indirubin l(-1) from 2.5 g L-tryptophan l(-1). CONCLUSION:The results suggest the cFMO can be used for the microbial production of both indigo and indirubin.
journal_name
Biotechnol Lettjournal_title
Biotechnology lettersauthors
Ameria SP,Jung HS,Kim HS,Han SS,Kim HS,Lee JHdoi
10.1007/s10529-015-1824-2subject
Has Abstractpub_date
2015-08-01 00:00:00pages
1637-44issue
8eissn
0141-5492issn
1573-6776journal_volume
37pub_type
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journal_title:Biotechnology letters
pub_type: 杂志文章
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pub_type: 杂志文章
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