Extracción y caracterización estructural de colágeno obtenido a partir de escamas de pescado mediante hidrólisis enzimática con corolasa.

Abstract

This research aimed to obtain collagen from fish scales through enzymatic hydrolysis using Corolase®, and to characterize the extracted product in terms of yield, and molecular structure. The selected fish scales had a high protein content (67.14 %), low fat content (0.05 %), and a significant level of minerals, requiring a prior demineralization step. Three enzymatic treatments were evaluated by varying the Corolase® concentration (5, 7, and 9 mL), under controlled conditions of pH (8.0–9.0), temperature (55 °C), and reaction time (6 hours). The hydrolysate was then subjected to centrifugation, lyophilization, sieving, and storage of the dry collagen for analysis. The treatment with 7 mL of enzyme was the most effective for collagen extraction, achieving the highest yield (60.19%) with statistically significant differences (p < 0.05) compared to the other treatments, according to ANOVA and Tukey’s test. Additionally, sample 7R1 showed the highest crystallinity index (86.01%) and the largest crystal size (5.77 nm) according to X-ray diffraction (XRD) analysis, indicating a more conserved and ordered molecular organization. Although sample 9R1 exhibited the most defined FTIR bands, the 7 mL condition represents the best balance between yield, structural quality, and industrial application potential of the extracted collagen. Overall, the findings demonstrate that Corolase® is an effective enzyme for marine collagen extraction, enabling high yield and good structural quality. The 7 mL condition proved to be the most balanced, making the obtained collagen suitable for cosmetic formulations that require solubility, purity, and conformational stability.