By-product of Korean liquor fermented by Saccharomyces cerevisiae exhibits skin whitening activity.

Herein, the skin whitening effect of the fermentation residue of Saccharomyces cerevisiae was investigated. The fermentation residue showed radical scavenging activity and attenuated tyrosinase activity. Furthermore, the fermentation residue of S. cerevisiae significantly suppressed melanin generation in B16F10 cells. Interestingly, the sample-containing formulation exhibited increased skin whitening activity compared with that by the control formulation in a clinical study. Notably, the endogenous tyrosinase expression was not altered by the fermentation residue of S. cerevisiae; however, the enzymatic activity of tyrosinase was inhibited. Furthermore, the sample did not change TRP1 and TRP2 expression in B16F10 cells. Thus, the fermentation residue of S. cerevisiae was assumed to directly suppress the tyrosinase enzyme. It was confirmed that the fermentation residue of S. cerevisiae was a competitive inhibitor of tyrosinase. Taken together, the fermentation residue of S. cerevisiae could be a novel skin whitening agent originating from the traditional Korean liquor production process. Supplementary Information: The online version contains supplementary material available at 10.1007/s10068-022-01062-7.

Umbilicaria esculenta Extract Exhibits Antiwrinkle Activity by Suppressing ErbB2 Phosphorylation.

Umbilicaria esculenta (UE), an edible lichen, is widespread in northeast Asian countries, including China, Japan, and Korea. In the present study, we examined the antiwrinkle activity of UE. We observed that the UE extract (UEE) suppressed ultraviolet (UV)-induced matrix metalloprotein-1 (MMP-1) expression and reactive oxygen species (ROS) generation in a human keratinocyte cell line (HaCaT) and human skin tissue. In addition, UEE reversed the UV-induced decrease in collagen in the human skin tissue. Excessive and chronic UV exposure is a key factor underlying skin wrinkle formation via MMP-1 expression. As treatment with UEE disrupted the UV-activated mitogen-activated protein kinase (MAPK) signaling pathway, we applied an antibody array to unveil the underlying mechanism of UEE. Interestingly, UEE treatment inhibited ErbB2 phosphorylation, but not epidermal growth factor receptor phosphorylation, a heterodimerization partner with ErbB2. Furthermore, UEE treatment enhanced UV-suppressed phosphatase activity via ROS suppression. Collectively, our findings indicate that UEE enhances ErbB2 dephosphorylation to suppress UV-induced MMP-1 expression.