摘要
以蚕丝断裂强力作为蚕丝织物酸水解老化样品老化程度的考核指标,利用衰减全反射傅里叶变换红外光谱(ATR-FTIR)技术和红外光谱去卷积拟合技术考察样品丝蛋白一级、二级结构的变化,分析丝蛋白β-折叠结构变化对蚕丝织物断裂强力的影响,同时利用X射线衍射(XRD)技术测试分析样品丝蛋白结晶度变化,以此探讨蚕丝织物的老化规律及老化机制。结果表明,随着蚕丝织物酸水解老化处理时间延长和氢离子浓度增加,丝蛋白的β-折叠结构相对含量呈下降趋势,而蚕丝织物断裂强力随老化处理时间的变化规律与丝蛋白β-折叠结构相对含量的变化有一致性。进一步分析蚕丝织物断裂强力变化曲线区域特性,发现丝蛋白β-折叠结构相对含量的变化是引起蚕丝织物断裂强力变化的主要原因,并且对样品丝蛋白结晶度的测试结果佐证了上述观点。
By taking breaking strength as evaluation index of aging degree for silk fabric sample undergone acid hydrolysis treatment, attenuated total reflectance Fourier transform infrared spectroscopy （ATR-FTIR） and infrared spectrometric self-deconvolution fitting approach were employed to examine primary and secondary structural change of the silk protein and to analyze impact of β-sheet structure change in the silk protein on breaking strength. Meanwhile, X-ray diffraction （XRD） technology was employed to test and analyze crystallinity variation of the silk protein sample so as to explore the aging regularity and mechanism of silk fabrics. The results showed that, as the time of aging treatment by acid hydrolysis prolonged and the concentration of hydrogen ion increased, the relative content of β-sheet structure in silk protein displayed a trend of decrease while the variation of breaking strength of the aging silk fabric with time of aging treatment was consistent with that of the relative content of β-sheet structure. Further analysis to sectional characteristics of the variation curves revealed that the relative content variation of β-sheet structure was the major cause to breaking strength variation of the silk fabrics, which was also verified by data from crystallinity determination to the silk protein sample.
出处
《蚕业科学》
CAS
CSCD
北大核心
2013年第1期100-105,共6页
ACTA SERICOLOGICA SINICA
基金
北京市教委科技发展面上项目(No.KM200810012003)
关键词
家蚕丝
酸水解老化
断裂强力
红外光谱
二级结构
Bombyx mori silk
Acid hydrolysis aging
Breaking strength
Infrared spectroscopy
Secondary structure
