Development of an effective method for the extraction of bioactive peptides from bovine bones

Abstract

The meat industry is estimated to produce millions of tons of meat by-products annually. However, the significant limitations to extracting the collagens from these meat by-products could be technological challenges and high costs. This study aimed to develop an efficient method for producing bioactive collagen peptides from meat by-products using a plant-derived enzyme extract as an alternative to commercial enzymes. For this study, bovine leg and brisket bones were used. Collagen hydrolysates from the bones were extracted using 10 mL/100g pineapple by-product extract (PE) or 500 mg/100 g pepsin. The use of PE resulted in a higher collagen yield compared to pepsin. Type-I and type-II collagens were the main components in the leg and brisket bones, respectively. Collagen products extracted with PE exhibited a broad range of molecular weights (50–10 kDa). Forty peptides were identified from the collagen products extracted with PE. Among them, the highest angiotensin-converting enzyme inhibitory activity was Gly-Ala-Arg (IC₅₀ at 168.95 μmol/L), followed by Gly-Pro-Met-Gly-Pro-Arg-Gly (IC₅₀ at 189.47 μmol/L), and Gly-Pro-Arg-Gly (IC₅₀ at 197.02 μmol/L). Notably, Gly-Pro-Met-Gly-Pro-Arg-Gly also showed the highest antioxidant activity. These findings suggest that PE could serve as a cost-effective alternative to commercial enzymes for developing the collagen hydrolysates industry from meat by-products.