Purification And Properties Of Collagen-Degrading Enzyme From Sea Cucumber Viscera
Keywords
Sea Cucumber, Internal Organs, Gelatin Zymogram, Metalloproteinase, Isolation And Purification
Abstract
In view of the autolysis phenomenon of sea cucumbers, the presence of proteases related to collagen degradation in sea cucumber viscera was studied in order to understand the role of endogenous proteases in the autolysis process of sea cucumbers and provide a theoretical basis for elucidating the intrinsic mechanism of autolysis. Through ammonium sulfate salting out, deae-sepharose anion exchange column chromatography, sephacryls-200 gel filtration column chromatography, phenylsepharoseff hydrophobic column chromatography and miniq ion exchange column chromatography, the gelatin-degrading gelatin was isolated and purified from sea cucumber viscera. Protease. The fluorescent substrate was used to study its enzymatic properties and its degradation of sea cucumber body wall collagen. The results show that the optimal temperature of the enzyme is 30¡ãC and the optimal pH is 7.5. It can be completely inhibited by metalloproteinase inhibitors edta and egta, and can also be completely inhibited by serine protease inhibitors such as pmsf and pefablocsc. The substrate specificity showed that the enzyme only decomposed the fluorescent substrate of metalloproteinase, and it was speculated that it was a metalloprotease. The enzyme can effectively decompose sea cucumber body wall collagen at both 4 and 37¡ãC, indicating that it plays an important role in the autolysis process of sea cucumbers.
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Original research was done by Ma Jinhua, Weng Ling, Yan Longjie, Zhang Lingjing, Liu Guangming, Cao Minjie
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