Catalyzes the oxidative cleavage of several carotenoids and apocarotenoids in vitro. In contrast to other carotenoid oxygenases, cleaves substrates at two different sites, namely the central C15-C15' and an excentric double bond at the C13-C14 position, leading to retinal (C20), beta-apo-14'-carotenal (C22) and beta-apo-13-carotenone (C18) from beta-carotene (C40), as well as the corresponding hydroxylated products from zeaxanthin and lutein. Converts beta-apo-10'-carotenal (C27) into beta-apo-13-carotenone (C18) and to minor amounts of beta-apo-15-carotenal (retinal; C20) from the cleavage at the C13-C14 and the C15-C15' double bonds, respectively. Can also cleave beta-apo-8'-carotenal, 3-OH-beta-apo-8'-carotenal and 3-OH-beta-apo-10'-carotenal. Does not use as substrates beta-apocarotenoids that have a chain length shorter than C25. Also cleaves lycopene into apo-13-lycopenone (C18) and apo-15'-lycopenal (acycloretinal, C20). Moreover, is able to cleave 3,3'-dihydroxy-isorenieratene representing aromatic carotenoids synthesized by other mycobacteria. Might be involved in the utilization of carotenoids from host cells to produce compounds required for normal growth. Binds 1 Fe(2+) ion per subunit. kcat is 393, 562, 1307 and 764 sec(-1) with beta-apo-8'-carotenal, beta-apo-10'-carotenal, 3-OH-beta-apo-8'-carotenal and 3-OH-beta-apo-10'-carotenal as substrate, respectively. M.tuberculosis is assumed to be unable to synthesize conventional colored carotenoids, but the data obtained in PubMed:20929460 reveal that M.tuberculosis may utilize carotenoids from host cells and interfere with their retinoid metabolism. The occurrence of suitable carotenoid-substrates (i.e. beta-carotene, lutein, zeaxanthin and lycopene) have been shown in human plasma and tissues, and the apocarotenoid substrate beta-apo-10'-carotenal may also be present in lungs. Belongs to the carotenoid oxygenase family.