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Lycopene‐accumulating E. coli transformed with human CMO II as a lycopene metabolism model
Author(s) -
Lu ChiHua,
Gong Xiaoming,
Marisiddaiah Raju,
Rubin Lewis P.,
Erdman John W.
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.34.4
Subject(s) - lycopene , chemistry , biochemistry , carotenoid , acetone
Mouse and ferret CMO II have been reported to asymmetrically cleave beta‐carotene or lycopene at the 9', 10' double bond and form apo‐10′‐carotenal or apo‐10′‐lycopenal. To investigate the ability of human CMO II to cleave lycopene, four E. coli strains were prepared: control, lycopene‐accumulating (LYC), lycopene‐accumulating transformed with human CMO II (Lyc‐CMO II), and lycopene‐accumulating transformed with an enzymatic site mutated human CMO II (Lyc‐mtCMO II). E coli were extracted with acetone by sonication, and lycopene metabolic products (lycopenoids) were determined by HPLC. PCR and western blot confirmed that the CMO II gene was successfully expressed in E. coli cells. Among the strains tested, Lyc‐mtCMO II accumulated the highest lycopene content, followed by LYC, Lyc‐CMO II, and control, while the lycopenoids, apo‐8′‐lycopenal, apo‐10′‐lycopenal, apo‐12′‐lycopenal, apo‐10′‐lycopenoic acid, and apo‐15′‐lycopenoic acid, were below limits of detection. (Supported by CA125384A, HD42174, and RR18728) Grant Funding Source CA125384A