Purification and characterization of a novel ?-carotene-9',10'-oxygenase from Saccharomyces cerevisiae ULI3.

ABSTRACT: A novel ?-carotene-9,10'-oxygenase (ScBCO2) has been characterized from Saccharomyces cerevisiae ULI3 to convert ?-carotene to ?-apo-10'-carotenal, which is a precursor of the plant hormone strigolactone.The ScBCO2 enzyme was purified to homogeneity by ammonium sulfate precipitation, Q sepharose and Superdex-200 chromatography. The molecular mass of the enzyme was ~50 kDa by SDS-PAGE. The purified ScBCO2 enzyme displayed optimal activity at 45 °C and pH 8. Tween 20 (1%, w/v), Trition X-100 (1%, w/v), Mg(2+) (5 mM), Zn(2+) (5 mM), Cu(2+) (5 mM), Ca(2+) (5 mM) or DTT (5 mM) increased in the activity by 3, 7, 14, 17, 23, 26 and 27%, respectively. ScBCO2 only exhibited cleavage activity towards carotenoid substrates containing two ?-ionone rings and its catalytic efficiency (kcat/Km) followed the order ?-carotene > ?-carotene > lutein.ScBCO2 could be used as a potential candidate for the enzymatic biotransformation of ?-carotene to ?-apo-10'-carotenal in biotechnological applications.

SUBMITTER: Wei T 

PROVIDER: S-EPMC4565880 | biostudies-other | 2015 Oct

REPOSITORIES: biostudies-other