RESUMEN
Collagen peptides play an important role in the increasing use of collagen peptides as dietary supplements in food and beverages and as bioactive ingredients in cosmetics, healthcare, and pharmaceuticals. Collagenase enzymatically cleaves gelatin to produce collagen polypeptides. However, the enzymatic activity of collagenase is very low (25900 U) and does not allow for adequate enzymatic digestion. Therefore, proteases are used to assist in enzymatic digestion. Porcine gelatin, bovine gelatin, and fish protein gum were enzymatically digested, and the content of collagen peptides in the enzymatically digested lyophilized powder was identified by high-performance liquid chromatography and mass spectrometry, and then the content of the desired collagen peptides was increased by isolation and purification, and the result of the determination was that the content of collagen peptides was the highest after enzymatic digestion and isolation and purification with the use of porcine gelatin as the raw material, and the content of the collagen peptides was about 45.47%. ß-nicotinamide mononucleotide (NMN) was mixed with the prepared samples to determine its antioxidant properties and ability to promote the growth of human dermal fibroblasts. The results showed that the antioxidant capacity was enhanced with the increase of collagen polypeptide content, and NMN could promote the scavenging of DPPH⢠and â¢OH free radicals by collagen polypeptides. The ability to promote the growth of human dermal fibroblasts was enhanced with the increase of collagen polypeptide content. This paper aimed to prepare a high content of collagen polypeptides from three raw materials, porcine gelatin, bovine gelatin, and fish protein gum, and further to determine the biological activities.