In vitro study of the carotenoid-cleavage enzyme from Staphylococcus pasteuri TS-82 revealed substrate specificities and generation of norisoprenoid flavors
Reactions of a crude enzyme extracted from S. pasteuri TS-82 to cleave carbon-carbon bonds in bicyclic and monocyclic carotenoid substrates were investigated. Dependencies of enzyme activities on processing temperature and pH were investigated and non-volatile and volatile breakdown products were characterized. The crude enzyme showed a maximum activity with zeaxanthin, followed in decreasing order by β-carotene, canthaxanthin, astaxanthin, and β-apo-8'-carotenal. The optimum pH value of the enzyme was 3.0 for both bicyclic and monocyclic substrates, whereas the optimum temperature of the enzyme was substrate specific at 60°C for C 40 carotenoids and 50°C for β-apo-8'-carotenal. Liquid Chromatography-Mass Spectra (LC-MS) and Gas Chromatography- Mass Spectra (GC-MS) indicated that the crude enzyme was able to catalyze substrates with cleavage at 9-10 and 9'-10' double bonds with C 13 norisoprenoids being the main volatile reaction products in each case. Astaxanthin is a major source for α,β-dihydro-β-ionone.
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