本文以猪皮胶原蛋白为原料，采用超高压协同稀盐酸诱导胶原明胶化。重点研究了不同诱导时间对胶原蛋白明胶化的分子机制的影响。处理时间5 min至30 min范围内，胶原的热变性温度Tm和热焓值rH均呈先下降后升高趋势，与明胶得率变化趋势一致。红外光谱（FT-IR）结果表明:超高压协同酸处理后大部分三螺旋结构被破坏，15 min处理对二级结构破坏最为严重，与得率变化趋势一致，说明胶原二级结构破坏程度与明胶得率相关。SDS-PAGE分析表明:超高压协同酸处理过程会降解胶原的亚基组分，不同处理时间对亚基组分破坏程度差别不明显，比较明胶化胶原和对应明胶的亚基组分含量，发现后期热处理后亚基组分降解程度很低，说明超高压协同酸处理抑制了热处理过程中亚基组分的过度降解。

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 andh HCl could inhibit the degradation of subunits during subsequent heating treatment.

国家自然科学基金项目（31301425）；重庆市高等学校优秀人才计划；中国博士后科学基金面上项目(2014M562267)；中央高校基本科研业务费重点项（2362014xk11）；重庆市特色食品工程技术研究中心能力提升项目（cstc2014pt-gc8001）