Collagen is the most abundant structural protein in animals, comprising approximately 30% of total protein content. It forms a triple-helical structure from three polypeptide chains rich in glycine, proline, and hydroxyproline residues, providing tensile strength to connective tissues including skin, bones, tendons, and cartilage. In food science, collagen is extracted from animal sources and partially hydrolyzed to produce gelatin, which is widely used as a gelling agent, stabilizer, and thickener in confectionery, dairy products, and supplements. Native collagen is insoluble in cold water but can be solubilized through acid or alkaline treatment and heat. It lacks a defined small-molecule structure, existing instead as high-molecular-weight polymers that denature above approximately 40°C. Hydrolyzed collagen peptides are bioavailable and commonly consumed for potential benefits to joint and skin health, supported by various clinical studies.