Characterization of a flavin-containing monooxygenase from Corynebacterium glutamicum and its application to production of indigo and indirubin.

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 Lett

journal_title

Biotechnology letters

authors

Ameria SP,Jung HS,Kim HS,Han SS,Kim HS,Lee JH

doi

10.1007/s10529-015-1824-2

subject

Has Abstract

pub_date

2015-08-01 00:00:00

pages

1637-44

issue

8

eissn

0141-5492

issn

1573-6776

journal_volume

37

pub_type

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