Sunday, July 29, 2007
P19

Characterization of beta-carotene 15,15'-monooxygenase from Mus musculus

Yeong-Su Kim1, Nam-Hee Kim1, Hye-Jung Kim1, Seon-Won Kim2, and Deok-Kun Oh1. (1) Department of Bioscience and biotechnology, Konkuk University, Seoul, South Korea, (2) Division of Applied Life Science, Gyeongsang National University, 900 Gajwadong, Jinju, 660-701, South Korea

Characterization of β-carotene 15,15'-monooxygenase

from Mus musculus

Yeong-Su Kim1, Nam-Hee Kim1, Hye-Jung Kim1, Seon-Won Kim2, Deok-Kun Oh1

1Department of Bioscience and biotechnology, Konkuk University, Seoul 143-701, Republic of Korea

2Division of Applied Life Science (BK21), EB-NCRC Gyeongsang National University, Jinju 660-701, Republic of Korea



The β-carotene 15,15'-monooxygenase, cleaves β-carotene into two molecules of retinal, catalyzes the first step in vitamin A synthesis. The β-carotene 15,15'-monooxygenase gene from Mus musculus was cloned into pET 24(a) vector and then expressed Escherichia coli. The expressed enzyme was purified by His-taq affinity and resource Q union exchange column chromatographies with a final specific activity of 0.505 units/g. The enzymatic activity of β-carotene 15,15'-monooxygenase to produce retinal from β-carotene was optimal at pH 9.0 and temperature 37 °C.


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