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Chelation of the Collagen Peptide of Seabass (Lates calcarifer) Scales with Calcium and Its Product Development
Seabass (Lates calcarifer) is one of the top farmed and raised fish in Taiwan, and fish scales are the main by-product after processing. Fish scales contain high amounts of collagen, which can chelate with minerals and enhance mineral absorption in the human body. Hence, fish scales from seabass were enzymatically hydrolyzed to obtain seabass scale collagen peptide (SBSCP). Calcium, the most consumed mineral supplement, was chelated with SBSCP to form SBSCP-Ca. The optimal conditions for chelation were a peptide/calcium ratio: 1:1 (w/w), pH 5.0, and 50 °C for 20 min. The conjugated sites were carboxyl and amino groups based on Fourier transform infrared (FTIR) spectroscopy. Scanning electronic microscope/energy-dispersive X-ray spectroscopy (SEM/EDS) evidently showed the alternation of SBSCP’s molecular structure after chelation and increased concentrations of metal ions. SBSCP-Ca was stable up to 90 °C and from pH 2.0 to 5.0. The retention rate was 70%, as determined after in vitro digestion. The extracts of blackcurrant or berry-grape seeds were added to neutralize the fishy odor and provide antioxidant ability for commercialization. This is the first complete study of the characteristics of SBSCP-Ca as well as their commercialization.
Chelation of the Collagen Peptide of Seabass (Lates calcarifer) Scales with Calcium and Its Product Development
Seabass (Lates calcarifer) is one of the top farmed and raised fish in Taiwan, and fish scales are the main by-product after processing. Fish scales contain high amounts of collagen, which can chelate with minerals and enhance mineral absorption in the human body. Hence, fish scales from seabass were enzymatically hydrolyzed to obtain seabass scale collagen peptide (SBSCP). Calcium, the most consumed mineral supplement, was chelated with SBSCP to form SBSCP-Ca. The optimal conditions for chelation were a peptide/calcium ratio: 1:1 (w/w), pH 5.0, and 50 °C for 20 min. The conjugated sites were carboxyl and amino groups based on Fourier transform infrared (FTIR) spectroscopy. Scanning electronic microscope/energy-dispersive X-ray spectroscopy (SEM/EDS) evidently showed the alternation of SBSCP’s molecular structure after chelation and increased concentrations of metal ions. SBSCP-Ca was stable up to 90 °C and from pH 2.0 to 5.0. The retention rate was 70%, as determined after in vitro digestion. The extracts of blackcurrant or berry-grape seeds were added to neutralize the fishy odor and provide antioxidant ability for commercialization. This is the first complete study of the characteristics of SBSCP-Ca as well as their commercialization.
Chelation of the Collagen Peptide of Seabass (Lates calcarifer) Scales with Calcium and Its Product Development
Xiu-Hui Yang (author) / Yu-Tung Chen (author) / Jen-Min Kuo (author) / Shih-Gao Chou (author) / Chia-Min Lin (author)
2023
Article (Journal)
Electronic Resource
Unknown
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