鱼鳞酶溶性胶原蛋白的体外自组装影响因素研究

Study on the factors influencing the self-assembly of the pepsin-soluble collagen from fish scale

天然胶原蛋白具有良好的生物安全性、相容性和促细胞增殖能力,作为功能材料应用于食品、医学美容、组织工程领域成为近年来的研究热点。分子自组装是胶原蛋白的固有性质,是其作为功能材料的理论基础。以鲢鱼鱼鳞为原料,通过清洗、晾干后用胃蛋白酶提取胶原蛋白的方法,研究超声处理、缓冲体系、温度、pH值、离子种类、离子强度、胶原蛋白浓度等对胶原蛋白自组装的影响。实验结果表明:样品的超声处理和溶液中的Ca^2+对自组装有抑制作用,一定范围内温度的升高、胶原蛋白浓度的增加、Na^+与PBS缓冲液都对胶原蛋白体外自组装有促进作用,p H7.3时自组装能力最强,离子强度对自组装并无明显作用。

Natural collagen has good biological safety, compatibility and ability to promote cell proliferation. As a functional material, it has become a research hotspot in the fields of food, medical cosmetology and tissue engineering in recent years. Molecular self-assembly is an inherent property of collagen, which is the theoretical basis of collagen as a functional material. In this paper, the collagens were extracted with pepsin from the silver carp scales after their being cleaned and dried, then the influence of factors such as ultrosonication, buffer system, temperature, pH, ion species, ionic strength and collagen concentration on the self-assembly of collagen was investigated. The results indicated that the ultrasonication and the Ca^2+ in the solution had inhibitory effect on the self-assembly. While increasing the temperature and the concentration of collagen, and Na^+ and PBS buffer all promoted the in vitro self-assembly of collagen. The collagen had the strongest self-assembly at pH7.3, and the ionic strength had no obvious effect on the self-assembly of the collagen.