Extraction and Characterization of Collagens from Abalone Muscle
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Abstract:
Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were extracted from abalone (Haliotis discus hannai) muscle, and their physicochemical properties were investigated and compared. The results showed that the extraction yield of ASC from abalone muscle was 0.63%, which was lower than that of any PSC extracted at different pepsin concentrations. Amino acid composition analysis showed that the Gly content of both ASC and PSC were less than one-third of the total amino acids; however, both ASC and PSC contained 12.03~16.30 Cys residues and 9.75~14.68 Tyr residues per 1000 residues. The results of sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis indicated that the α subunits of ASC were composed of α1 (160 ku), α2 (140 ku), and α3 (130 ku), but there were only three α1 peptide chains found in PSC. The maximum ultraviolet absorption of ASC was observed at 224 nm, while that of PSC shifted to 228 nm. Significant differences were observed between the viscosity of ASC and PSC; thus, the denaturation temperature of ASC was higher than that of any PSC. Based on the results of zeta potential measurement, both PSC and ASC had a similar isoelectric point at approximately pH 4.90. The effects of pH and NaCl concentration on the solubility of ASC were similar to those of PSC. However, at the same pH or NaCl concentration, the solubility of PSC was higher than that of ASC, and it was further increased to a certain extent with increasing pepsin concentration. In conclusion, these results suggest that the physicochemical properties of ASC and PSC from abalone muscle differ significantly.
