Enhanced production of sulforaphane by exogenous glucoraphanin hydrolysis catalyzed by myrosinase extracted from Chinese flowering cabbage (Brassica rapa var. parachinensis)

Sulforaphane formation via endogenous route is known to be less effective. Exogenous hydrolysis of the sulforaphane precursor is therefore of interest. Here, myrosinase activity was first determined to identify a suitable source of the enzyme from selected Brassica vegetables. Extracted enzyme was then evaluated for its thermal stability to establish a condition for extraction. Chinese flowering cabbage was selected as the source of myrosinase; suitable extraction condition was at 40 °C for 90 min. Enzyme extract was used to hydrolyze glucoraphanin standard into sulforaphane at 30 °C and pH 6. Exogenous hydrolysis reached the equilibrium with the reverse reaction after 30 min; sulforaphane concentration remained unchanged afterward. Molar fractional conversion of glucoraphanin into sulforaphane at 30-min hydrolysis was around 48%. In comparison with exogenous hydrolysis by myrosinase extracted from broccoli, which indeed exhibits higher activity than the enzyme extracted from Chinese flowering cabbage, no conversion of glucoraphanin into sulforaphane was unexpectedly observed.