Comparative Study On The Properties Of Enzymatically Soluble Collagen From Sea Cucumber Body Wall And Tilapia Skin
Keywords
Enzyme-Soluble Collagen, Sea Cucumber, Tilapia, Amino Acids, Structure
Abstract
This experiment conducted a comparative study on the physical and chemical properties of sea cucumber body wall enzymatically soluble collagen (pepsin soluble collagen from Stichopus japonicus, sjPSC) and tilapia skin enzymatically soluble collagen (pepsin soluble collagen from Oreochromis niloticus, onPSC). The results showed that the UV and Fourier transform infrared spectroscopic analysis results of the two collagens were relatively similar. It can be seen from the sodium dodecyl sulfate-polyacrylamide gel electrophoresis pattern that both collagens are dominated by ¦Á- and ¦Â-chains. Under non-reducing and reducing conditions, the electrophoresis patterns of the two are very similar, which shows that No disulfide bonds in the protein are reduced. Glycine is the main amino acid in sjPSC and onPSC, and each 1?000 amino acid residue contains (344.57¡À2.16) and (353.00¡À4.84) glycine residues respectively. In comparison, the contents of glutamic acid, aspartic acid, serine, valine, isoleucine and tyrosine in sjPSC are higher, while the contents of L-hydroxyproline, L-proline and leucine in onPSC are higher. The content of acid, phenylalanine, histidine and lysine is high. Under the action of V8 enzyme and ¦Á-chymotrypsin, peptide mapping analysis of sjPSC and onPSC showed that there are certain differences in the structures of the two, especially glutamic acid, aspartic acid and hydroxyproline residues
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Original research was done by Yu Cuiping, Wu Haitao, Tang Yue, Sun Na, Zhang Zhengyu, Li Aoting, Li Weikun, Wang Fenglin
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