L-半胱氨酸为还原剂从兔毛纤维中提取角蛋白
Extraction of Keratin from Rabbit Hair Using L-cystein as Reductive Agent
黎淑婷 1张毅 1张昊 1张睿1
作者信息
- 1. 天津工业大学 纺织学院,天津 300387
- 折叠
摘要
以L-半胱氨酸为还原剂从兔毛纤维中提取角蛋白,在最佳提取条件:pH=10.5,L-半胱氨酸浓度0.165 mol/L、尿素浓度8 mol/L、反应时间5 h、反应温度75 ℃,兔毛纤维溶解率高达74.12%.溶解液通过透析、冷冻干燥后,得到的角蛋白回收率为69.23%,角蛋白质量分数高达99.38%.通过SDS-聚丙烯酰胺凝胶电泳(SDS-PAGE)测定兔毛角蛋白的相对分子质量主要集中在11 kDa左右.利用XRD、FTIR、拉曼光谱以及差示扫描量热仪(DSC)表征分析角蛋白内部结构,结果表明,随着兔毛纤维的溶解,L-半胱氨酸破坏了兔毛纤维大分子链中35%(摩尔分数)的二硫键,导致角蛋白的二级结构发生变化,α-螺旋结构含量减少,α-结晶区含量降低,β-折叠结构含量增加.
Abstract
L-cystein was used as reductive agent to extract keratin from rabbit hair.Under the optimum conditions of pH value 10.5,L-cystein 0.165 mol/L,urea 8 mol/L,dissolving at 75 ℃ for 5 h,the dissolution rate of rabbit hair was up to 74.12%.Additionally,the recovery rate of final keratin was 69.23% after dialysis of the above dissolved solution and freeze drying,and the mass fraction of keratin was as high as 99.38%.The relative molecular mass of rabbit hair keratin was mainly concentrated in about 11 kDa via sodium dodecyl sulfate polyacrylamide gel electrophoresis(SDS-PAGE).The internal structure of keratin was characterized by X-ray diffraction(XRD),Fourier transform infrared(FTIR) spectroscopy,Raman spectroscopy and differential scanning calorimetry(DSC).The results indicated that as the rabbit hair dissolved,about 35%(mole fraction) disulfide bond in the rabbit hair was destroyed by L-cystein,which resulted in changes of secondary structure of keratin,in which the content of α-helix structure and α-crystalline region decreased,while the content of β-sheet structure increased.
关键词
兔毛/角蛋白/L-半胱氨酸/提取/表征Key words
rabbit hair/keratin/L-cystein/extraction/characterization引用本文复制引用
基金项目
中国农业部财政部国家级兔产业技术体系建设专项项目(CARS-44-D-2)
出版年
2017
NETL
NSTL
维普
万方数据