Physicochemical Properties and Biocompatibility Evaluation of Collagen from the Skin of Giant Croaker ( Nibea japonica )

• Published in: Marine drugs Vol. 16; no. 7; p. 222
• Main Authors: Tang, Yunping, Jin, Shujie, Li, Xiaoyan, Li, Xiaojuan, Hu, Xuyang, Chen, Yan, Huang, Fangfang, Yang, Zuisu, Yu, Fangmiao, Ding, Guofang
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 29.06.2018; MDPI
• Subjects: Analytical methods; Biocompatibility; characterization; Collagen; Collagen (type I); cosmetics; Cytotoxicity; Denaturation; Electrophoresis; Evaluation; Fourier transforms; Gel electrophoresis; Gels; Glycerol; Hydroxylation; Lead; Mercury; Mercury (metal); Moisture absorption; Nibea; Nibea japonica; Pepsin; Peptides; Physicochemical processes; Physicochemical properties; Proline; Protein denaturation; Skin; Sodium; Sodium dodecyl sulfate; Sodium lauryl sulfate; collagen; Nibea japonica; biocompatibility; characterization; cosmetics
• ISSN: 1660-3397; 1660-3397
• DOI: 10.3390/md16070222

Collagen and collagen peptides are widely used as cosmetic ingredients. In the present study, acid-solubilized collagen (ASC) and pepsin-solubilized collagen (PSC) were extracted from giant croaker ( ) skin. The proline hydroxylation rates of ASC and PSC were 38.1% and 39.3%. The denaturation temperatures (T ) were approximately 34.5 °C for both ASC and PSC. The results of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and fourier transform infrared spetroscopy (FTIR) demonstrated that ASC and PSC were mainly type I collagen. Furthermore, As, Pb and Hg contents in the extracted collagen were lower than the national standards of China. In addition, collagen had good moisture absorption and retention properties when compared to glycerol. The collagen was also not cytotoxic to NIH-3T3 fibroblast cells, indicating that skin collagen can be utilized in cosmetic applications.