甲酸对丝素蛋白结晶结构转变的影响  

Effect of formic acid on the crystalline structure transformation of silk protein

作　　者：梁苏平 何秀萍 牛翔宇 宁晚娥[1,2] 王倩 黄继伟[1,2,3] LIANG Suping;HE Xiuping;NIU Xiangyu;NING Wan’e;WANG Qian;HUANG Jiwei(College of Biological and Chemical Engineering,Guangxi University of Science and Technology,Liuzhou 545006,China;Rainbow Modern Textile Industry College,Guangxi University of Science and Technology,Liuzhou 545006,China;College of Textile and Clothing Engineering,Soochow University,Suzhou 215123,China)

机构地区：[1]广西科技大学生物与化学工程学院,广西柳州545006 [2]广西科技大学天虹现代纺织产业学院,广西柳州545006 [3]苏州大学纺织与服装工程学院,江苏苏州215123

出　　处：《丝绸》2024年第3期44-54,共11页Journal of Silk

基　　金：国家自然科学基金项目(51763001,51963002);广西自然科学基金项目(2016GXNSFBA380015);广西研究生教育创新计划项目(YCSW2023476)。

摘　　要：结晶结构是丝素蛋白材料表征的重要内容,对丝素蛋白结晶结构的认识和调控是制备高性能材料的基础。甲酸作为一种可溶解蚕丝的优良溶剂,所制备的再生丝素蛋白材料具有优异的性能,其根源与甲酸对丝素蛋白具有促结晶的作用有关。文章对比分析了基于氯化钙-甲酸溶剂溶制再生丝素蛋白膜与基于三元溶剂溶制再生丝素蛋白膜的结晶结构差异,并利用α-糜蛋白酶从基于三元溶剂制备的丝素蛋白水溶液中分离出高结晶部分和低结晶部分,随后分别利用甲酸和乙醇对分离所得高结晶部分和低结晶部分进行处理,对比分析了乙醇和甲酸对其结晶结构转变的影响。结果表明,相对于乙醇处理,甲酸具有更显著的促丝素蛋白结晶的作用,更有利于丝素蛋白从无规卷曲或Silk I结晶态转变为SilkⅡ结晶态。As a natural polymer protein,silk fibroin,with its excellent biocompatibility,controllable biodegradability,non-toxicity and low immunogenicity,has a wide range of applications in the fields of biomedical engineering materials,flexible wearable sensor devices,food and pharmaceuticals,and fine chemicals.In these engineering applications,silk fibroin is required to have certain mechanical properties and biomedical engineering application performance,and these properties and performance are closely related to the crystalline structure of silk fibroin protein,and the regulation of its mechanical properties can be realized by modulating the crystalline morphology or crystalline structure parameters in silk fibroin protein materials to meet the needs of biomedical engineering applications.The regulation of the crystalline structure of silk fibroin protein materials can be realized by adopting different solvent solutions and post-treatment processes.The silk fibroin protein material prepared by dissolving the aqueous solution of degummed silk with a ternary solvent(a solvent system consisting of calcium chloride,ethanol and water with molar ratio of 1 ∶2 ∶8) exhibits water solubility,low crystallinity,and is of the Silk I or amorphous mainly crystalline structure.It needs to be post-treated with a certain concentration of ethanol to realize the regulation of its crystalline structure,so as to achieve certain mechanical properties and water stability of the material.On the other hand,the silk fibroin primary material prepared with formic acid as solvent has a highly crystalline structure of Silk II and does not require any post-treatment.This suggests that formic acid also has the effect of promoting the crystallization of silk fibroin proteins,but there are few reports on the study of formic acid promoting the crystallization of silk fibroin proteins.To illustrate the effect of formic acid on the crystalline structure of silk fibroin proteins and the role of formic acid in promoting the crystallization of silk fibro

关 键 词：丝素蛋白 结晶结构 甲酸 促结晶作用 Α-糜蛋白酶 

分 类 号：TS102.33[轻工技术与工程—纺织工程]