Research & Reviews : Journal of Food Science & Technology Original Research Open Access

Exploring Chicken Sternal Cartilage as an Alternative Source of Bioactive Protein Hydrolysates

  1. Karina Pinheiro Martins Department of Food Science, Federal University of Technology
  2. Thaysa Fernandes Moya Moreira Department of Food Science, State University of Maringá (UEM)
  3. Anielle de Oliveira Department of Biochemistry (PBQ), State University of Maringá
  4. Valéria Maria Costa Teixeira Department of Food Science, Instituton Politécnico de Bragança
  5. Odinei Hess Gonçalves Department of Textile Engineering (DET), Department of Food Science, Federal University of Santa Catarina
  6. Rafael Porto Ineu Department of Food Technology and Science, Center of Rural Sciences, Federal University of Santa Maria
  7. Fernanda Vitória Leimann Department of Food Technology and Science, Center of Rural Sciences, Federal University of Santa Maria

Abstract

There is a growing concern on the correct use and dispose of the by-products of the food industry, and chicken slaughterhouse, such as cartilage, combs, and wattles may be strong candidates as a protein source for bioactive peptides, however it is crucial to understand how the proteolysis process may affect the peptide profile and their bioactivity. The objective of this work was to obtain protein hydrolysates from chicken sternal cartilage using Alcalase and Flavourzyme as catalysts and to determine their antioxidant capacity and acetylcholinesterase (AChE) inhibition potential. The cartilage was hydrolyzed with Alcalase (pH 8, 50°C, 1.8 wt%enzyme:substrate, substrate dry basis) and Flavourzyme (pH 7, 50°C; 1.8 wt%enzyme:substrate, substrate dry basis). Alcalase demonstrated a greater capacity for cartilage digestion (97.42% yield), and the resulting cartilage hydrolyzed a 1.8-fold higher capacity for AChE inhibition than Flavourzyme-catalyzed hydrolysate. On the other hand, Flavourzyme produced a hydrolysate with a 1.3-fold higher capacity on TBARS inhibition (74.2%) than Alcalase. The hydrolysates' amino acid profiles were delineated via HPLC, revealing the presence of 18 amino acids, notably, tryptophan, tyrosine, and histidine exhibited similar concentrations across the hydrolysates. The tryptophan/LNNA (large neutral amino acids) ratio was elevated in the hydrolysate generated by Flavourzyme, potentially correlating with its heightened TBARS reduction potential. Furthermore, the increased total amino acid content observed in the hydrolysate produced with Alcalase may be linked to its efficacy in AChE inhibition

Keywords

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