Enzymatic asymmetric cleavage of aquatic products-derived carotenoids and the bio-modulating mechanism of the enzymolysis products

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CMO2, betaCarotene 9, 10 monooxygenase, exhibits wide substrate specificity, and it can metabolize xanthophyll as well as betacarotene. We investigated whether CMO2 could cleave aquatic products derived carotenoids through evaluating CMO2 activity in mouse liver homogenate, the activity of recombinant CMO2, and CMO2 activity using CMO2 expressing cultured cells. We, however, could not detect the CMO2 activity in mouse liver homogenate. Although recombinant human CMO2 was produced by Baculotechnologies Company Limited, enzymatically active CMO2 was not obtained. According to a previous report, MDA MB 231, human breast cancer cell line, expresses CMO2, and then, we used this cell line in order to evaluate the CMO2 activity. We could detect no CMO2 metabolites accumulated in carotenoid treated MDA MB 231.