超高压处理对羊骨胶原蛋白三级结构的影响

Effect of Ultra-high Pressure Treatment on Tertiary Structure of Sheep Bone Collagen

以羊骨胶原蛋白为研究对象,研究不同超高压压力对胶原蛋白微观形态、热变性温度、吡啶交联物以及空间结构的影响。试验结果表明:超高压处理的胶原蛋白的微观形态在压力100~300 MPa时出现短暂的聚合现象;当压力超过400 MPa时胶原蛋白结构又重新展开。差式扫描量热仪(DSC)结果显示:经超高压处理的胶原蛋白的变性温度由44.9℃(对照组)降为31.7℃;胶原蛋白吡啶交联物羟赖氨酸吡啶啉(HP)和赖氨酸吡啶啉(LP)的含量随超高压压力的增加、保压时间的延长而显著下降(P<0.05);HP和LP与超高压压力和保压时间呈极显著负相关(P<0.01)。

Sheep bone collagen was used as the research object to explore the effects of different ultra-high pressure on the microstructure,thermal denaturation temperature,pyridine cross linkers of collagen and the changes of collagen spatial structure.The results showed that the micromorphology of ultra-high treated collagen polymerizes temporarily at a pressure of 100-300 MPa.When the pressure exceeded 400 MPa,the collagen structure expands again.DSC results showed that the denaturation temperature of collagen after ultra-high pressure treatment decreased from 44.9℃(control group)to 31.7℃.The contents of hydroxyl sine pyridine(HP)and lysine pyridine(LP),the cross-linkers of collagen pyridine,were significantly decreased with the increasing of ultra-high pressure pressure and the prolonging of pressure holding time(P<0.05).HP and LP were negatively correlated with ultra-high pressure and holding time(P<0.01).