Abstract
The conversion of beta-carotene to retinal by a recombinant beta-carotene 15,15'-dioxygenase (Blh protein) from an unculturable marine bacterium was optimized in aqueous solution. Toluene was optimal solvent for the dissolution of beta-carotene and the optimal solution for the conversion reaction contained 2.4% (w/v) Tween 20, 0.15 U enzyme/ml, and 350 mg beta-carotene/l. Under these conditions, the enzyme produced 181 mg retinal/l after 20 h. This is the highest reported value for the retinal concentration from beta-carotene.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacteria / enzymology*
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Bacteria / genetics
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Bacterial Proteins / genetics
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Bacterial Proteins / isolation & purification
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Bacterial Proteins / metabolism
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Biotransformation
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Cloning, Molecular
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Escherichia coli / genetics
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Retinaldehyde / metabolism*
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Seawater / microbiology
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beta Carotene / metabolism*
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beta-Carotene 15,15'-Monooxygenase / genetics
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beta-Carotene 15,15'-Monooxygenase / isolation & purification
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beta-Carotene 15,15'-Monooxygenase / metabolism*
Substances
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Bacterial Proteins
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Recombinant Proteins
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beta Carotene
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beta-Carotene 15,15'-Monooxygenase
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Retinaldehyde