皮革科学与工程 ›› 2019, Vol. 29 ›› Issue (05): 5-.

• 论文 •    下一篇

基于转谷氨酰胺酶交联胶原凝胶的结构与性能研究

  

  1. 四川大学皮革化学与工程教育部重点实验室;四川大学制革清洁技术国家工程实验室;
  • 出版日期:2019-10-12 上线日期:2019-10-12
  • 基金资助:
    国家自然科学基金资助项目(21776184)

Structure and Properties based on Collagen Gels Cross -linked with Microbial Transglutaminase

  1. 1. The Key Laboratory of Leather Chemistry and Engineering of Ministry of Education, Sichuan University, Chengdu 610065, China;2. National Engineering Laboratory for Clean Technology of Leather Manufacture, Sichuan University, Chengdu 610065, China)
  • Online:2019-10-12 Published:2019-10-12

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摘要： 采用微生物来源的转谷氨酰胺酶(MTG)对胶原凝胶进行交联改性,考察不同浓度的MTG(0.02～0.28 U/m L)对胶原凝胶结构和性能的影响,通过测量比较胶原凝胶的外观、红外光谱图、耐热稳定性、耐体外酶解能力、凝胶强度、吸水膨胀率,来表征改性前后胶原凝胶结构和性能的变化。结果表明:当MTG浓度为0.04 U/mL时,改性后胶原凝胶的性能最优。改性后的凝胶外观变化不明显,红外光谱分析表明胶原的三股螺旋结构未被破坏。当MTG浓度为0.04 U/mL时,比未改性的样品的耐热分解能力提高了11.79%,抗体外酶降解率提高了10.21%、凝胶强度提高了324 g,吸水膨胀率提高了1.65×103%,热变性温度略有增加。

关键词: 胶原凝胶, 转谷氨酰胺酶, 交联, 性能

Abstract: Collagen gels were prepared through the cross-linking with microbial transglutaminase (MTG). The effect of different concentrations of microbial transglutaminase on the structure and properties of collagen gels were studied, mainly concentrating on the appearance, FI -IR, thermal stability, enzymatic resistance, gel strength and water absorption of the gels. The results of thermal stability, enzymatic resistance, gel strength and water absorption of the gels showed that the optimum condition for cross-linking of collagen gel was 0.04 U/mL MTG. There was no obviously changed in the appearence of collagen gels, the FI-IR showed that the triple helix structure of collagen was maintained integrity. At the optimum concentration of MTG, the residual weight of thermogravimetric, the enzymatic resistance degradation ratio in vitro, the gel strength and the water absorption ratio increased by 11.79%, 10.21%, 324 g and 1.65 *103 % compared with those of uncross -linked collagen gel, respectively. However, the thermal denaturation temperature slightly increased.

Key words: collagen gels, microbial transglutaminase, cross-linking, properties

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