Physicochemical Characterization and In Vitro Skin-Related Biological Activities of Hydrolyzed Collagen Derived from Chicken Sternum

Hydrolyzed collagen preparations have attracted increasing attention because their biological properties may vary according to collagen source, peptide composition, and physicochemical characteristics. In this study, Richi I II III Collagen (HTCP), a hydrolyzed type I, II, and III collagen preparation derived from chicken sternum (keel) and manufactured by CNABIOTECH Co., Ltd. (Cheongju-si, Republic of Korea), was physicochemically characterized and evaluated for antioxidant and skin-related biological activities. Physicochemical characterization included analyses of amino acid composition and molecular weight distribution, while biological activities were assessed using ABTS and DPPH radical scavenging assays and human skin cell-based models. HTCP showed distinct responses in the two radical scavenging assays, with ABTS radical scavenging activity reaching 80.4 ± 0.0% at 100 mg/mL, whereas DPPH radical scavenging activity remained comparatively low (13.1 ± 4.6%). No cytotoxicity was detected in human dermal fibroblasts (HDF) or human epidermal keratinocytes (HEKn) at the concentrations tested. HTCP exhibited 101.65 ± 1.28% collagenase inhibition at 10% and significantly increased type I collagen, type III collagen, elastin, hyaluronic acid (HA), HAS2, and HAS3 levels, while reducing MMP-1 and HYAL1 levels. Collectively, these findings demonstrate changes in selected ECM- and HA-related protein levels in human skin cells following HTCP treatment under in vitro conditions, supporting further investigation of HTCP as a collagen-derived ingredient for skin-related applications.