食品科学

• 基础研究 • 上一篇    下一篇

草鱼皮胶原的体外自组装动力学研究

赵 燕,鲁 亮,杨 玲,邓明霞,杨 欢,汪海波   

  1. 武汉轻工大学食品科学与工程学院,湖北 武汉 430023
  • 出版日期:2014-06-15 发布日期:2014-07-03

Self-Assembly Kinetics of Collagen from Grass Carp Skin

ZHAO Yan, LU Liang, YANG Ling, DENG Ming-xia, YANG Huan, WANG Hai-bo   

  1. Collage of Food Science and Technology, Wuhan Polytechnic University, Wuhan 430023, China
  • Online:2014-06-15 Published:2014-07-03

摘要:

体外自组装是天然胶原的重要分子行为特征之一,并对胶原基产品性能产生显著影响。以草鱼皮酶溶性胶原蛋白为研究对象,重点开展胶原体外自组装动力学行为、影响因素、组装纤维的微观结构及其热稳定性能研究。浊度实验和自组装程度分析的结果表明,草鱼皮胶原蛋白具备体外自组装能力,其自组装进程受胶原质量浓度、pH值、离子强度、温度等因素的影响。在pH 7~8、胶原质量浓度3~5 mg/mL、体系温度25~30 ℃以及NaCl浓度0~200 mmol/L条件下胶原自组装进程较快、自组装程度较高;组装动力学分析的结果表明,在较高的离子强度(NaCl浓度300 mmol/L)和较低的组装温度(20 ℃)时,胶原组装进程表现为:成核、组装和平衡3 个阶段,而在较高组装温度(25~30 ℃)和较低离子强度时(NaCl浓度0~200 mmol/L),胶原组装进程表现为:快速组装段、低速组装段和平衡段;胶原纤维形态学观察结果表明,草鱼皮胶原组装纤维具有典型的D周期特征但D周期长度值(64.6 nm)小于哺乳动物胶原纤维(约67 nm);示差扫描量热法(differential scanning calorimetry,DSC)分析结果表明,经纤维重组后,草鱼皮胶原蛋白的热稳定性得到明显提升。

关键词: 淡水鱼, 胶原蛋白, 自组装, 动力学

Abstract:

In this study, the kinetic behavior and influential factors of self-assembly, fiber morphology and thermal stability
of pepsin soluble collagen from grass carp skin were explored. The turbidity and self-assembly degree indicated that grass
carp skin collagen had self-assembling ability although it was influenced by collagen concentration, pH, ionic strength and
temperature. Under the conditions of 7–8, 3–5 mg/mL, 25–30 ℃ and 0–200 mmol/L for pH, collagen concentration, culture
temperature and NaCl concentration, respectively the self-assembling process progressed faster and finally reached a higher
level. The kinetic analysis suggested that the whole assembly reaction could be divided into nucleating, fibrillogenesis and
plate phases at higher ionic strength and lower temperature, but divided into rapid assembly, slow assembly, and plate phases
when the assembling conditions were changed to lower ionic strength and higher temperature. Morphological observations
indicated that grass carp skin collagen could be self-assembled into fibrils with characteristic D-periodicity in vitro, but the
length of D-periodicity (64.6 nm) was smaller than that of the mammalian counterpart (approximately 67 nm). The results of
DSC analysis showed that the thermal stability of grass carp skin collagen was obviously improved after self-assembly.

Key words: fresh water fish, collagen, self-assembly, kinetics