Myrosinase

Myrosinase (thioglucoside glucohydrolase, EC 3.2.1.147) is a plant-derived enzyme responsible for hydrolyzing glucosinolates such as glucoraphanin into bioactive isothiocyanates, most notably sulforaphane. This reaction occurs naturally when plant tissues containing glucosinolates and myrosinase are disrupted, as in chewing or processing[2][4][5]. While cooking often deactivates plant myrosinase, some conversion of glucoraphanin to sulforaphane can also be mediated by the gut microbiota in mammals[1][2][4][6]. Myrosinase is not a direct therapeutic target but plays a central biochemical role in generating bioactive dietary metabolites that have been researched for anticancer, antioxidative, and anti-inflammatory properties via modulation of biological pathways such as Nrf2 activation[2][6]. The interindividual efficiency of glucoraphanin conversion via myrosinase is variable and can be enhanced by co-administration of exogenous myrosinase (from sources like mustard seed) or by maintaining gut microbiota populations capable of this activity[1][3][4].

Other names

Thioglucoside glucohydrolaseEC 3.2.1.147

Hydrolysis of the thioglucoside bond in glucosinolates (such as glucoraphanin), resulting in the formation of bioactive isothiocyanates (such as sulforaphane)[2][4][6]