期刊
BIOTECHNOLOGY LETTERS
卷 37, 期 8, 页码 1637-1644出版社
SPRINGER
DOI: 10.1007/s10529-015-1824-2
关键词
Corynebacterium glutamicum; Flavin-containing monooxygenase; Indigo; Indirubin; Maltose-binding protein; Monooxygenase
资金
- Basic Science Research Program through the National Research Foundation of Korea (NRF) - Ministry of Education, Science and Technology [NRF-2012R1A1A2007229]
- National Research Foundation of Korea [2012R1A1A2007229] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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. 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 A degrees C and pH 8. From absorption spectrum analysis, the cFMO was classified as a flavoprotein. FMO activity was strongly inhibited by 1 mM Cu2+ 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). The results suggest the cFMO can be used for the microbial production of both indigo and indirubin.
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