ABSTRACT:
Collagen is the extracellular matrix component and is essential in maintaining skin health. Native collagen is too large to penetrate the skin epidermis when applied topically. Therefore, a protein size reduction through hydrolysis is required. The hydrolyzed product of collagen is greatly influenced by the hydrolysis method. Hydrolyzed collagen is a low molecular peptide that can penetrate the skin to increase its effectiveness as antiaging. This study aimed to compare peptide fish collagen's thermal and enzymatic hydrolysis and characterize the hydrolysates. Thermal and enzymatic processes hydrolyzed the fish collagen. The fish collagen was incubated at various temperatures (50, 60, 70, 80, 90, and 100°C) for different time incubation (1, 2, 3, 4, and 5hours) for thermal hydrolysis. Enzymatic hydrolysis was conducted by incubating fish collagen with bromelain (10U/ml) at 50°C for an hour. The peptide was characterized with electrophoresis, Lowry, hydroxyproline content, SEM (scanning electron microscope), FTIR (Fourier transform infrared), and DSC (differential scanning calorimetry). Thermal hydrolysis with variations in temperature and incubation time produces denaturized protein. Enzymatic hydrolysis with bromelain produces collagen peptides. The hydrolysis of collagen resulted in the different characteristics of hydrolyzed collagen. As seen from SEM analysis, the enzymatic hydrolysis is smaller than native. The DSC and FTIR analysis confirmed the change in physical traits between native and enzymatic hydrolysis of collagen. Collagen hydrolysate is obtained through enzymatic hydrolysis with bromelain; the observed degree of hydrolysis is 60%. Taken together, enzymatic hydrolysis was a suitable method to produce peptide collagen.