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

ABSTRACT:

Objectives

A novel β-carotene-9,10'-oxygenase (ScBCO2) has been characterized from Saccharomyces cerevisiae ULI3 to convert β-carotene to β-apo-10'-carotenal, which is a precursor of the plant hormone strigolactone.

Results

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 β-ionone rings and its catal

SUBMITTER: Wei T 

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

REPOSITORIES: biostudies-literature