Extraction and characterization of biomaterials from pork bones: a potential alternative of pineapple by-product extract for commercial proteases.

This study aimed to develop cost-effective methods for extracting biomaterials from pork bones. Collagen and chondroitin sulfate (CS) were extracted from pork bones using a pineapple by-product extract (PE) at 5% (v/w) or commercial proteases (pepsin and Alcalase) under identical conditions. The use of PE resulted in a higher collagen yield than pepsin (3.77% vs. 1.42%). The CS concentration extracted with PE was comparable to that obtained using Alcalase (11.98 mg/g vs. 11.37 mg/g). Protein pattern analysis indicated that collagens extracted using either PE or pepsin were type I collagen. 1H NMR analysis showed that CS extracted using either PE or Alcalase contained both CS-C and CS-A units. Among 28 peptides identified, 7 peptides (Gly-Arg, Glu-Gly-Arg, Ala-Val-Gly, Leu-Ala, Leu-Val-Gly, Phe-Ala-Gly-Gly, and Gly-Pro-Leu-Gly-Pro-Hyp-Gly-Ala-Pro-Gly) and 4 peptides (Leu-Pro, Leu-Thr-Gly, Gly-Pro-Leu-Gly-Pro-Hyp-Gly-Ala-Pro-Gly, and Gly-Pro-Ala-Gly-Pro-Val-Gly-Pro-Val-Gly) were found only in the collagen extracted with pepsin and PE, respectively. Notably, peptide hydrolysates derived from PE-extracted collagen exhibited higher free radical scavenging and ferrous ion-chelating activities than those obtained from pepsin-extracted collagen. Overall, PE emerges as a cost-effective and efficient alternative to commercial enzymes for extracting biomaterials from pork bones.