Tyrosinase inhibitory performance of hydrolysate from post-washing liquor of steam exploded corn stalk and its fractionation enhancement

In this work, corn stalk was subjected to steam explosion (SE) pretreatment, and the hydrolysate in post-washing liquor of steam exploded corn stalk was assayed for anti-tyrosinase activity for the first time. The hydrolysate showed strong anti-tyrosinase activity with an IC50 of 2.17 mg/mL (inhibitor concentration when 50% of tyrosinase activity is inhibited) at SE severity of 4.20 (198 degrees C, 20 min). Through hydrolysate component profiles and model substance analysis, phenolic compounds (especially lignin-derived H-unit monomers and phenolic acids) were confirmed to be the major tyrosinase inhibitors in hydrolysate. To further improve the inhibitory activity, an enrichment process of phenolic compounds by ethyl-acetate fractionation of hydrolysate was employed. Ethyl-acetate soluble fraction exhibited significantly enhanced anti-tyrosinase activity (IC50, 0.29 mg/mL), which was even better than p-coumaric acid (a typical tyrosinase inhibitor with IC50 of 0.31 mg/mL). Additionally, the mixed-type inhibition of hydrolysate on tyrosinase was illustrated by kinetics study and the interaction between hydrolysate and tyrosinase was confirmed by fluorescence quenching measurement. Consequently, this work aims to evaluate and improve the anti-tyrosinase activity of hydrolysate from steam explosion processing of corn stalk, which opens new perspectives in potential application of currently underused corn stalk hydrolysate as a value-added tyrosinase inhibitor.