The Molecular Mechanism Of Ultrahigh Pressure Exposure Time Affecting Collagen Gelatinization
Keywords
Porcine Skin Collagen Gelatinization Molecular Mechanismporcine Skin Collagen Gelatinization Molecular Mechanism
Abstract
This article uses pig skin collagen as raw material, and uses ultrahigh pressure and dilute hydrochloric acid to induce collagen gelatinization. The focus was on the effects of different induction times on the molecular mechanism of collagen gelatinization. Within the treatment time range of 5 min to 30 min, the thermal denaturation temperature Tm and heat enthalpy value rH of collagen first decreased and then increased, which was consistent with the change trend of gelatin yield. Infrared spectroscopy (FT-IR) results show that most of the triple helical structure is destroyed after ultrahigh pressure collaborative acid treatment, and the 15 min treatment causes the most severe damage to the secondary structure, which is consistent with the yield change trend, indicating that the degree of damage to the secondary structure of collagen is related to Gelatin yield related. SDS-PAGE analysis showed that the ultra-high pressure synergistic acid treatment process will degrade the subunit components of collagen, and there is no obvious difference in the degree of destruction of subunit components at different treatment times. Comparing the subunit component content of gelatinized collagen and corresponding gelatin, it was found that The degree of degradation of subunit components after late heat treatment was very low, indicating that ultrahigh pressure synergistic acid treatment inhibited excessive degradation of subunit components during heat treatment. Ultra-high pressure (UHP) with dilute hydrochloric acid (HCl) was used to induce the gelatinization of collagen derived from porcine skin. The effects of various processing times on the molecular mechanism of collagen gelatinization were investigated. The denaturation temperature (Tm) and enthalpy (rH) of gelatinized collagen initially decreased followed by an increase as the processing time increased from 5 to 30 min, which also corresponded with the increased gelatin yield. FT-IR showed that the triple helix in the gelatinized collagen was almost completely damaged. The secondary structures were partly retained and the highest amount of damage was observed after 15 min of treatment. This was also consistent with the gelatin yield, which possibly imply that the secondary structures of collagen are correlated with the gelatin yield. SDS-PAGE analysis indicated that the subunit compositions of collagen were degraded during the UHP in presence of dilute HCl, but the extent of damage was similar in treatments that were conducted for 5 to 30 min. Compared with the gelatinized collagen, less subunit compositions were damaged during the heating treatment , which indicated that the treatment via a combination of UHP and h HCl could inhibit the degradation of subunits during subsequent heating treatment.
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Original research was done by Yu Wei
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