Comparative Study On The Thermal Stability Of Insoluble Collagen Fibers And Enzymatically Soluble Collagen From Jellyfish Fimbriae
Keywords
Rhopilema Esculentum Insoluble Collagen Fibril (Icf) Pepsin-Solubilized Collagen (Psc) Two-Dimensional Fourier Transform Infrared Spectroscopy (2D-Ftir) Thermal Stability
Abstract
Jellyfish (Rhopilema esculentum) is an important large-scale economic jellyfish produced in my country’s traditional fishery. Its umbrella is rich in collagen, but collagen is sensitive to heat. Research on its thermal stability is crucial to the development and utilization of jellyfish resources. In this paper, insoluble collagen fibers (ICF) and enzymatic soluble collagen (PSC) were extracted from the jellyfish fimbriae, and their thermal stability was comparatively analyzed. The results show that the amino acid composition and molecular mass of jellyfish ICF and PSC are similar to type I collagen, and their higher-order structural differences also lead to differences in thermal stability. Fourier transform infrared spectroscopy (FT-IR) research found that when heated to 36¡ãC, the infrared absorption of the amide I band of PSC suddenly decreased, and the structure changed significantly, while when the ICF temperature increased to 50¡ãC, the infrared absorption of the amide I band The absorption just started to change slightly, and the thermal stability of ICF was better than that of PSC. Two-dimensional infrared analysis found that the 3?10-helical structure in PSC and the ¦Â-sheet structure (low frequency) in ICF are most sensitive to temperature changes. In addition to the automatic peak, there are several cross-peaks in both PSC and ICF, indicating that during the heat treatment process There are intramolecular and intermolecular interactions between various structures. This study provides a certain theoretical basis for the development and utilization of jellyfish collagen. Rhopilema esculentum, a large jellyfish, is one of the most economically important traditional fishery products in China. The umbrellas of jellyfish are rich in collagen. Since collagen is temperature-sensitive, it is important to study its thermal stability for the development and utilization of jellyfish resources. In this study, insoluble collagen fibrils (ICFs) and pepsin-solubilized collagen (PSC) were extracted from umbrellas of Rhopilema esculentum, and their thermostability was compared. The results indicated that the amino acid compositions and molecular weights of the ICF and PSC were similar to those of type I collagen, and the differences in the higher-order structure of ICF and PSC led to their different thermal stabilities. Fourier transform infrared spectroscopy (FT-IR) analysis showed that the intensity of the amide I band in the infrared absorption of PSC decreased rapidly, and apparent structural changes occurred when the sample was heated to 36 ¡æ. When the temperature was raised to 50 ¡æ, the intensity of the amide I band of ICF changed only slightly, suggesting that thermal stability of ICF is superior to that of PSC. Two-dimensional infrared analysis revealed that 310-helical structures in PSC and ¦Â-sheets (low frequency) in ICF were sensitive to temperature changes. In addition to the automatic peak, there were a number of overlapping peaks , revealing that there were some intramolecular and intermolecular interactions among different higher-order structures during the heating process. This study provides a theoretical basis for the development and utilization of jellyfish collagen.
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Original research was done by Wang Xusong
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