Study On The Extraction And Properties Of Abalone Muscle Collagen
Keywords
Abalone Muscle Acid-Soluble Collagen Pepsin-Soluble Collagen Pepsin Concentration Physicochemical Properties Abalone Muscle Acid-Soluble Collagen Pepsin-Soluble Collagen Pepsin Concentration Physicochemical Properties
Abstract
Abalone muscle acid-soluble collagen (ASC) and enzyme-soluble collagen (PSC) at different pepsin mass concentrations were extracted, and their physical and chemical properties were studied and compared. It was found that the extraction rate of ASC was only 0.63%, which was lower than that of any PSC. The amino acid composition results show that the Gly content of ASC and PSC does not reach 1/3 of the total amino acids, but both contain 12.03~16.30 Cys residues and 9.75~14.68 Tyr residues. According to the SDS-PAGE spectrum, it was found that the ¦Á subunit of abalone muscle ASC is composed of 160 ku ¦Á1, 140 ku ¦Á2 and 130 ku ¦Á3 peptide chains, while PSC is composed of three ¦Á1 peptide chains. The maximum UV absorption peak of ASC appears at 224 nm, while that of PSC is shifted to 228 nm. There are obvious differences in viscosity properties between ASC and PSC, which results in the thermal denaturation temperature of ASC being higher than that of either PSC. Zeta potential measurement results show that the isoelectric point of both ASC and PSC is around pH 4.90. The trend of the influence of pH and NaCl on the solubility of ASC is basically the same as that of PSC. However, at the same pH or NaCl concentration, the solubility of PSC is higher than that of ASC, and it increases to a certain extent as the amount of pepsin added increases. In summary, there are obvious differences in the physical and chemical properties of abalone muscle ASC and PSC. 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 ¦Á subunits of ASC were composed of ¦Á1 (160 ku), ¦Á2 (140 ku), and ¦Á3 (130 ku), but there were only three ¦Á1 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.
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Original research was done by Ma Shaokang
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