摘要
采用熔融尿素和蛋白酶处理羊毛提取角蛋白,羊毛溶解率分别达到99.6%和88.9%,产率分别为89.5%和86.2.%,均好于还原法。2种方法所得角蛋白的分子量分布为45.3~66.2 kD和<2 kD,分别对应于角蛋白大分子和角蛋白肽。红外光谱(ATR-FTIR)、X射线衍射(XRD)和热重分析(TGA)结果显示,提取所得角蛋白的分子结构与羊毛基本相同,尿素法角蛋白分子中二硫键未发生断裂,酶法角蛋白分子中二硫键部分断裂;尿素法和蛋白酶法角蛋白质的结晶度均较高,分别为30.14%和45.14%;其热稳定性稍有差异,总失重率分别为79.71%和87.23%,前者热稳定性较好,后者热稳定性较差。
Molten urea (U)and enzyme (E) were used in the extraction of wool keratin. The solubility of wool and the yield of keratin were 99.6% and 89.5% in U-method, 88.9% and 86.2% in E-method. These two approaches behaved better than that of reductive method. The molecular weight distribution was 45.0 ~ 66.2 kD and 〈 2 kD, which corresponding to keratin-protein and keratin-peptide. The results of ATR-FTIR, WXRD and TGA indicated that the molecular structure of keratin was almost the same as wool, in addition, the characteristic disulfide bonds were remained in U-keratin, while in E-keratin they were partly broken in the pretreatment. The crystallinity of these two types of keratin were both relatively high, 30. 14% and 45.14% respectively. There was a little difference in the thermal stability between U-keratin and E-keratin, the former was good and the latter was relatively poor.
出处
《毛纺科技》
CAS
北大核心
2013年第5期1-6,共6页
Wool Textile Journal