利用付立叶红外光谱与付立叶拉曼光谱初探超细羊毛粉的光谱行为

Study on the Spectroscopic Behavior of Super-fine Wool Powder by FT-IR and FT-Raman Spectroscopy

采用付立叶红外(FT-IR)和付立叶拉曼(FT-Raman)光谱仪,对美利奴原毛、机械磨碎羊毛粉、氯化或氧化预处理后经酶水解的超细羊毛粉进行分析。研究结果表明:机械磨碎羊毛粉,其化学结构与原毛相比无明显变化;氯化或氧化预处理后经酶水解的超细羊毛粉的IR谱图发生了较大的变化,羊毛大分子中胱氨酸最终氧化为磺基丙氨酸,且原胱氨酸二硫键发生了断裂,生成新的半胱氨酸磺酸盐;同时预处理时间越长,羊毛粉的平均直经越小,新产生的1 044 cm-1、1 026 cm-1吸收信号也越强。

Merino wool, machine grinding wool powder and their super-fine wools, which are subjected to enzymic hydrolysis after chloridation and oxidation pretreatment, were studied with FT-IR and FT- Raman spectroscopy. The results show that the chemical structure of machine-grinding wool changes hardly compared with the raw wool, however, the IR spectra for super-fine wools alter greatly. It indicates that cystine in wool polymer turns into sulfuric alanine and the S-S bond in cystine breaks and yields diame cm^-1 semi-cystine sulphate. Moreover, ter of the wool powder is and the the longer the pretreatment time is, the smaller the mean stronger the new absorption peak is at 1 044 cm^-1 and 1 021cm^-1.