Changes In Molecular Structure Of Collagen During Gelatinization
Keywords
Collagen Gelatin Gelatinization Microstructurecollagen Gelatin Gelatinization Microstructure
Abstract
This experiment uses pig skin collagen as raw material to study the changes in the microstructure of collagen during the gelatinization process. Research shows that under the induction of 8 hours of acid treatment, the degree of gelatinization of collagen is high, and the gelatin yield after hot water extraction can reach 83.98%. As the acid treatment time is further extended, the gelatin yield decreases significantly; differential calorimetry scanning (DSC), infrared spectroscopy (FTIR) and circular dichroism spectroscopy (CD) studies show that as acid treatment proceeds, the triple helix structure of collagen gradually loosens, and the valence bonds that maintain the stability of the triple helix structure are gradually destroyed. After 8 hours of acid treatment, , the excessive destruction of the collagen triple helix structure is the main reason for the decrease in gelatin yield. Polyacrylamide gel electrophoresis (SDS-PAGE) analysis showed that during acid treatment, degradation of collagen peptide chains always existed, and the amount of subunits retained in gelatinized collagen directly affected the subunit content in gelatin. Therefore, a balance must be found between the degradation of the peptide chain and the loosening of the triple helix structure during the gelatinization process to obtain high yield and high-quality gelatin. The microstructure of collagen from pig skin was studied during gelatinization. The results showed that a relatively high degree of gelatinization of collagen was achieved after 8-h acid treatment and the yield of gelatin reached 83.98% after hot water extraction, while the yield of gelatin dropped significantly with increasing duration of acid treatment. The results from differential scanning calorimetry (DSC), Fourier transform infrared spectroscopy (FT-IR), and circular dichroism (CD) revealed that the triple-helical structure of collagen became progressively loose and valence bonds stabilizing the triple-helix were gradually destroyed during the process of acid treatment. The triple-helical structure was excessively destroyed after 8-h acid treatment, which could be the main reason for the decrease in gelatin yield. Moreover, the results of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) indicated that collagen peptide chains were degraded during acid treatment and the gelatin subunit content was directly influenced by the amount of subunits that remained after gelatinization. Therefore, during the gelatinization of collagen, a balance between subunit Degradation and the loosening of the triple-helical structure are required, in order to obtain high yield of high-quality gelatin.
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Original research was done by Wang Xuemeng
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