Retinal production from beta-carotene by beta-carotene 15,15'-dioxygenase from an unculturable marine bacterium.
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.
Department of Bioscience and Biotechnology, Konkuk University, 1 Hwayang-dong, Gwangjin-gu, Seoul, 143-701, Republic of Korea.
Yeong-Su
YS
Kim
Chang-Su
CS
Park
Deok-Kun
DK
Oh
D001419:Bacteria / Q000201:enzymology* / Q000235:genetics; D001426:Bacterial Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D001711:Biotransformation; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism; D012172:Retinaldehyde / Q000378:metabolism*; D012623:Seawater / Q000382:microbiology; D019207:beta Carotene / Q000378:metabolism*; D050559:beta-Carotene 15,15'-Monooxygenase / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D019207:beta Carotene; D050559:beta-Carotene 15,15'-Monooxygenase; D012172:Retinaldehyde