KMID : 1007520160250010221
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Food Science and Biotechnology 2016 Volume.25 No. 1 p.221 ~ p.227
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n vitro Study of the Carotenoid-cleavage Enzyme from Staphylococcus pasteuri TS-82 Revealed Substrate Specificities and Generation of Norisoprenoid Flavors
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Zhu Ming-Ming
Wang Shu-Lin Fan Ming-Tao Li Jing
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Abstract
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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 ¥â-carotene, canthaxanthin, astaxanthin, and ¥â-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¡ÆC for C40 carotenoids and 50¡ÆC for ¥â-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 C13 norisoprenoids being the main volatile reaction products in each case. Astaxanthin is a major source for ¥á,¥â-dihydro-¥â-ionone.
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KEYWORD
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Staphylococcus pasteuri TS-82, crude enzyme, carotenoids, aroma compounds
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