Discovery of superior bioactive peptides of two edible Lentinus mushrooms protein hydrolysate in biological activities: tyrosinase inhibitory and antioxidant activity

This study investigated protein hydrolysates obtained from Lentinus squarrosulus and Lentinus edodes fruiting bodies via gastric protease hydrolysis and ultrafiltration, yielding peptides with a molecular weight below 6.5 kDa. These hydrolysates displayed significant tyrosinase inhibitory activity similar to positive controls, peptide from Chinese quince seed (RHAKF) and kojic acid. L. squarrosulus-derived hydrolysates exhibited superior antioxidant properties compared to L. edodes in DPPH (47% vs. 23%) and ABTS (77% vs. 23%) assays. Identified bioactive peptides, particularly LILGGSSS from L. squarrosulus, interacted with tyrosinase through hydrogen bonds at specific residues. Notably, these protein hydrolysates showcased potent tyrosinase inhibition without cytotoxic effects, presenting promising prospects for addressing hyperpigmentation caused by excessive tyrosinase activity from stress or UV exposure.